LIVIVO - Search results -

Search results

Result 1 - 10 of total 184

Search options

Article ; Online: Multiple masks of a Shigella podophage.

Jiang, Yong-Liang / Zhou, Cong-Zhao

Structure (London, England : 1993)

2024 Volume 32, Issue 1, Page(s) 1–2

Abstract: In this issue of Structure, Subramanian et al. present the cryo-EM structure of Shigella podophage HRP29, which possesses a T7-like tail complex surrounded by six P22/Sf6-like tailspikes and two unique decoration proteins. These colorful masks of HRP29 ... ...

Abstract	In this issue of Structure, Subramanian et al. present the cryo-EM structure of Shigella podophage HRP29, which possesses a T7-like tail complex surrounded by six P22/Sf6-like tailspikes and two unique decoration proteins. These colorful masks of HRP29 record the frequent events of horizontal gene transfer during evolution.
MeSH term(s)	Shigella/virology ; Bacteriophages/ultrastructure
Language	English
Publishing date	2024-01-05
Publishing country	United States
Document type	Journal Article
ZDB-ID	1213087-4
ISSN	1878-4186 ; 0969-2126
ISSN (online)	1878-4186
ISSN	0969-2126
DOI	10.1016/j.str.2023.12.002
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 4141: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Transport mechanism of human bilirubin transporter ABCC2 tuned by the inter-module regulatory domain.

Mao, Yao-Xu / Chen, Zhi-Peng / Wang, Liang / Wang, Jie / Zhou, Cong-Zhao / Hou, Wen-Tao / Chen, Yuxing

Nature communications

2024 Volume 15, Issue 1, Page(s) 1061

Abstract: Bilirubin is mainly generated from the breakdown of heme when red blood cells reach the end of their lifespan. Accumulation of bilirubin in human body usually leads to various disorders, including jaundice and liver disease. Bilirubin is conjugated in ... ...

Abstract	Bilirubin is mainly generated from the breakdown of heme when red blood cells reach the end of their lifespan. Accumulation of bilirubin in human body usually leads to various disorders, including jaundice and liver disease. Bilirubin is conjugated in hepatocytes and excreted to bile duct via the ATP-binding cassette transporter ABCC2, dysfunction of which would lead to Dubin-Johnson syndrome. Here we determine the structures of ABCC2 in the apo, substrate-bound and ATP/ADP-bound forms using the cryo-electron microscopy, exhibiting a full transporter with a regulatory (R) domain inserted between the two half modules. Combined with substrate-stimulated ATPase and transport activity assays, structural analysis enables us to figure out transport cycle of ABCC2 with the R domain adopting various conformations. At the rest state, the R domain binding to the translocation cavity functions as an affinity filter that allows the substrates of high affinity to be transported in priority. Upon substrate binding, the R domain is expelled from the cavity and docks to the lateral of transmembrane domain following ATP hydrolysis. Our findings provide structural insights into a transport mechanism of ABC transporters finely tuned by the R domain.
MeSH term(s)	Humans ; Adenosine Triphosphate/metabolism ; Bilirubin ; Cryoelectron Microscopy ; Multidrug Resistance-Associated Protein 2/genetics ; Multidrug Resistance-Associated Protein 2/metabolism
Chemical Substances	Adenosine Triphosphate (8L70Q75FXE) ; Bilirubin (RFM9X3LJ49) ; Multidrug Resistance-Associated Protein 2 ; ABCC2 protein, human
Language	English
Publishing date	2024-02-05
Publishing country	England
Document type	Journal Article
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-024-45337-5
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Modular catalytic activity of nonribosomal peptide synthetases depends on the dynamic interaction between adenylation and condensation domains.

Peng, Ye-Jun / Chen, Yuxing / Zhou, Cong-Zhao / Miao, Wei / Jiang, Yong-Liang / Zeng, Xiaoli / Zhang, Cheng-Cai

Structure (London, England : 1993)

2024 Volume 32, Issue 4, Page(s) 440–452.e4

Abstract: Nonribosomal peptide synthetases (NRPSs) are large multidomain enzymes for the synthesis of a variety of bioactive peptides in a modular and pipelined fashion. Here, we investigated how the condensation (C) domain and the adenylation (A) domain cooperate ...

Abstract	Nonribosomal peptide synthetases (NRPSs) are large multidomain enzymes for the synthesis of a variety of bioactive peptides in a modular and pipelined fashion. Here, we investigated how the condensation (C) domain and the adenylation (A) domain cooperate with each other for the efficient catalytic activity in microcystin NRPS modules. We solved two crystal structures of the microcystin NRPS modules, representing two different conformations in the NRPS catalytic cycle. Our data reveal that the dynamic interaction between the C and the A domains in these modules is mediated by the conserved "RXGR" motif, and this interaction is important for the adenylation activity. Furthermore, the "RXGR" motif-mediated dynamic interaction and its functional regulation are prevalent in different NRPSs modules possessing both the A and the C domains. This study provides new insights into the catalytic mechanism of NRPSs and their engineering strategy for synthetic peptides with different structures and properties.
MeSH term(s)	Microcystins ; Peptide Synthases/chemistry ; Molecular Conformation ; Peptides
Chemical Substances	non-ribosomal peptide synthase (EC 6.3.2.-) ; Microcystins ; Peptide Synthases (EC 6.3.2.-) ; Peptides
Language	English
Publishing date	2024-02-09
Publishing country	United States
Document type	Journal Article
ZDB-ID	1213087-4
ISSN	1878-4186 ; 0969-2126
ISSN (online)	1878-4186
ISSN	0969-2126
DOI	10.1016/j.str.2024.01.010
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 4141: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Profiling the interplay and coevolution of

Wang, Xiao-Qian / Du, Kang / Chen, Chaoyi / Hou, Pu / Li, Wei-Fang / Chen, Yuxing / Li, Qiong / Zhou, Cong-Zhao

Microbiology spectrum

2024 , Page(s) e0029824

Abstract: The cyanosiphophage Mic1 specifically infects the bloom-forming : Importance: The highly ... ...

Abstract	The cyanosiphophage Mic1 specifically infects the bloom-forming Importance: The highly polymorphic
Language	English
Publishing date	2024-05-02
Publishing country	United States
Document type	Journal Article
ZDB-ID	2807133-5
ISSN	2165-0497 ; 2165-0497
ISSN (online)	2165-0497
ISSN	2165-0497
DOI	10.1128/spectrum.00298-24
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article: Structural insights into cyanobacterial RuBisCO assembly coordinated by two chaperones Raf1 and RbcX.

Li, Qiong / Jiang, Yong-Liang / Xia, Ling-Yun / Chen, Yuxing / Zhou, Cong-Zhao

Cell discovery

2022 Volume 8, Issue 1, Page(s) 93

Abstract: RuBisCO is the most abundant enzyme in nature, catalyzing the fixation of ... ...

Abstract	RuBisCO is the most abundant enzyme in nature, catalyzing the fixation of CO
Language	English
Publishing date	2022-09-20
Publishing country	England
Document type	Journal Article
ISSN	2056-5968
ISSN	2056-5968
DOI	10.1038/s41421-022-00436-9
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Herbal small RNAs in patients with COVID-19 linked to reduced DEG expression.

Qiao, Xiangyu / Huang, Fengming / Shi, Xiaohu / Deng, Xingyu / Zhang, Cong / Mei, Song / Wang, Zhiqing / Zhou, Congzhao / Jiang, Chengyu / Tan, Xinghua

Science China. Life sciences

2023 Volume 66, Issue 6, Page(s) 1280–1289

Abstract: In China, more than 80% of patients with coronavirus disease 2019 (COVID-19) received traditional Chinese medicine (TCM) as a treatment and their clinical efficacy have been reported. However, the underlying molecular mechanism remains unclear. Previous ... ...

Abstract	In China, more than 80% of patients with coronavirus disease 2019 (COVID-19) received traditional Chinese medicine (TCM) as a treatment and their clinical efficacy have been reported. However, the underlying molecular mechanism remains unclear. Previous studies have identified herbal small RNAs (sRNAs) as novel functional components. In this study, a cohort of 22 patients with COVID-19 treated with Toujie Quwen (TQ) granules was analyzed. We observed thousands of herbal small RNAs that entered the blood cells of patients after the consumption of TQ granules. In response to this treatment, the reduced differentially expressed genes (DEGs) were highly correlated with the predicted target genes of the most prevalent herbal sRNAs detected in the blood. Moreover, the predicted target genes of the top 30 sRNAs from each of the 245 TCMs in the Bencao sRNA Atlas overlapped with 337 upregulated DEGs in patients with mild COVID-19, and 33 TCMs, with more than 50% overlapping genes were identified as effective TCMs. These predicted target genes of top 30 sRNAs from Juhong, Gualoupi and Foshou were confirmed experimentally. Our results not only elucidated a novel molecular mechanism of TCM potential clinical efficacy for COVID-19 patients, but also provided 33 effective COVID-19 TCMs for prescription optimization.
MeSH term(s)	Humans ; COVID-19 ; Drugs, Chinese Herbal/pharmacology ; Drugs, Chinese Herbal/therapeutic use ; SARS-CoV-2/genetics ; Medicine, Chinese Traditional ; RNA
Chemical Substances	Drugs, Chinese Herbal ; RNA (63231-63-0)
Language	English
Publishing date	2023-02-03
Publishing country	China
Document type	Journal Article
ZDB-ID	2546732-3
ISSN	1869-1889 ; 1674-7305
ISSN (online)	1869-1889
ISSN	1674-7305
DOI	10.1007/s11427-022-2225-3
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Allosteric regulation of nitrate transporter NRT via the signaling protein PII.

Li, Bo / Wang, Xiao-Qian / Li, Qin-Yao / Xu, Da / Li, Jing / Hou, Wen-Tao / Chen, Yuxing / Jiang, Yong-Liang / Zhou, Cong-Zhao

Proceedings of the National Academy of Sciences of the United States of America

2024 Volume 121, Issue 11, Page(s) e2318320121

Abstract: Coordinated carbon and nitrogen metabolism is crucial for bacteria living in the fluctuating environments. Intracellular carbon and nitrogen homeostasis is maintained by a sophisticated network, in which the widespread signaling protein PII acts as a ... ...

Abstract	Coordinated carbon and nitrogen metabolism is crucial for bacteria living in the fluctuating environments. Intracellular carbon and nitrogen homeostasis is maintained by a sophisticated network, in which the widespread signaling protein PII acts as a major regulatory hub. In cyanobacteria, PII was proposed to regulate the nitrate uptake by an ABC (ATP-binding cassette)-type nitrate transporter NrtABCD, in which the nucleotide-binding domain of NrtC is fused with a C-terminal regulatory domain (CRD). Here, we solved three cryoelectron microscopy structures of NrtBCD, bound to nitrate, ATP, and PII, respectively. Structural and biochemical analyses enable us to identify the key residues that form a hydrophobic and a hydrophilic cavity along the substrate translocation channel. The core structure of PII, but not the canonical T-loop, binds to NrtC and stabilizes the CRD, making it visible in the complex structure, narrows the substrate translocation channel in NrtB, and ultimately locks NrtBCD at an inhibited inward-facing conformation. Based on these results and previous reports, we propose a putative transport cycle driven by NrtABCD, which is allosterically inhibited by PII in response to the cellular level of 2-oxoglutarate. Our findings provide a distinct regulatory mechanism of ABC transporter via asymmetrically binding to a signaling protein.
MeSH term(s)	Nitrate Transporters ; Nitrates/metabolism ; Bacterial Proteins/metabolism ; Allosteric Regulation ; Cryoelectron Microscopy ; Cyanobacteria/metabolism ; Adenosine Triphosphate/metabolism ; Nitrogen/metabolism ; Carbon/metabolism ; PII Nitrogen Regulatory Proteins/genetics ; PII Nitrogen Regulatory Proteins/metabolism
Chemical Substances	Nitrate Transporters ; Nitrates ; Bacterial Proteins ; Adenosine Triphosphate (8L70Q75FXE) ; Nitrogen (N762921K75) ; Carbon (7440-44-0) ; PII Nitrogen Regulatory Proteins
Language	English
Publishing date	2024-03-08
Publishing country	United States
Document type	Journal Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2318320121
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1148: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Structure of the intact tail machine of Anabaena myophage A-1(L).

Yu, Rong-Cheng / Yang, Feng / Zhang, Hong-Yan / Hou, Pu / Du, Kang / Zhu, Jie / Cui, Ning / Xu, Xudong / Chen, Yuxing / Li, Qiong / Zhou, Cong-Zhao

Nature communications

2024 Volume 15, Issue 1, Page(s) 2654

Abstract: The Myoviridae cyanophage A-1(L) specifically infects the model cyanobacteria Anabaena sp. PCC 7120. Following our recent report on the capsid structure of A-1(L), here we present the high-resolution cryo-EM structure of its intact tail machine including ...

Abstract	The Myoviridae cyanophage A-1(L) specifically infects the model cyanobacteria Anabaena sp. PCC 7120. Following our recent report on the capsid structure of A-1(L), here we present the high-resolution cryo-EM structure of its intact tail machine including the neck, tail and attached fibers. Besides the dodecameric portal, the neck contains a canonical hexamer connected to a unique pentadecamer that anchors five extended bead-chain-like neck fibers. The 1045-Å-long contractile tail is composed of a helical bundle of tape measure proteins surrounded by a layer of tube proteins and a layer of sheath proteins, ended with a five-component baseplate. The six long and six short tail fibers are folded back pairwise, each with one end anchoring to the baseplate and the distal end pointing to the capsid. Structural analysis combined with biochemical assays further enable us to identify the dual hydrolytic activities of the baseplate hub, in addition to two host receptor binding domains in the tail fibers. Moreover, the structure of the intact A-1(L) also helps us to reannotate its genome. These findings will facilitate the application of A-1(L) as a chassis cyanophage in synthetic biology.
MeSH term(s)	Myoviridae ; Capsid Proteins/chemistry ; Capsid ; Anabaena
Chemical Substances	Capsid Proteins
Language	English
Publishing date	2024-03-26
Publishing country	England
Document type	Journal Article
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-024-47006-z
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Structure and assembly of the α-carboxysome in the marine cyanobacterium Prochlorococcus.

Zhou, Rui-Qian / Jiang, Yong-Liang / Li, Haofu / Hou, Pu / Kong, Wen-Wen / Deng, Jia-Xin / Chen, Yuxing / Zhou, Cong-Zhao / Zeng, Qinglu

Nature plants

2024 Volume 10, Issue 4, Page(s) 661–672

Abstract: Carboxysomes are bacterial microcompartments that encapsulate the enzymes RuBisCO and carbonic anhydrase in a proteinaceous shell to enhance the efficiency of photosynthetic carbon fixation. The self-assembly principles of the intact carboxysome remain ... ...

Abstract	Carboxysomes are bacterial microcompartments that encapsulate the enzymes RuBisCO and carbonic anhydrase in a proteinaceous shell to enhance the efficiency of photosynthetic carbon fixation. The self-assembly principles of the intact carboxysome remain elusive. Here we purified α-carboxysomes from Prochlorococcus and examined their intact structures using single-particle cryo-electron microscopy to solve the basic principles of their shell construction and internal RuBisCO organization. The 4.2 Å icosahedral-like shell structure reveals 24 CsoS1 hexamers on each facet and one CsoS4A pentamer at each vertex. RuBisCOs are organized into three concentric layers within the shell, consisting of 72, 32 and up to 4 RuBisCOs at the outer, middle and inner layers, respectively. We uniquely show how full-length and shorter forms of the scaffolding protein CsoS2 bind to the inner surface of the shell via repetitive motifs in the middle and C-terminal regions. Combined with previous reports, we propose a concomitant 'outside-in' assembly principle of α-carboxysomes: the inner surface of the self-assembled shell is reinforced by the middle and C-terminal motifs of the scaffolding protein, while the free N-terminal motifs cluster to recruit RuBisCO in concentric, three-layered spherical arrangements. These new insights into the coordinated assembly of α-carboxysomes may guide the rational design and repurposing of carboxysome structures for improving plant photosynthetic efficiency.
Language	English
Publishing date	2024-04-08
Publishing country	England
Document type	Journal Article
ISSN	2055-0278
ISSN (online)	2055-0278
DOI	10.1038/s41477-024-01660-9
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Structural insights into the activation of autoinhibited human lipid flippase ATP8B1 upon substrate binding.

Cheng, Meng-Ting / Chen, Yu / Chen, Zhi-Peng / Liu, Xin / Zhang, Zhiyong / Chen, Yuxing / Hou, Wen-Tao / Zhou, Cong-Zhao

Proceedings of the National Academy of Sciences of the United States of America

2022 Volume 119, Issue 14, Page(s) e2118656119

Abstract: SignificanceATP8B1 is a P4 ATPase that maintains membrane asymmetry by transporting phospholipids across the cell membrane. Disturbance of lipid asymmetry will lead to the imbalance of the cell membrane and eventually, cell death. Thus, defects in ATP8B1 ...

Abstract	SignificanceATP8B1 is a P4 ATPase that maintains membrane asymmetry by transporting phospholipids across the cell membrane. Disturbance of lipid asymmetry will lead to the imbalance of the cell membrane and eventually, cell death. Thus, defects in ATP8B1 are usually associated with severe human diseases, such as intrahepatic cholestasis. The present structures of ATP8B1 complexed with its auxiliary noncatalytic partners CDC50A and CDC50B reveal an autoinhibited state of ATP8B1 that could be released upon substrate binding. Moreover, release of this autoinhibition could be facilitated by the bile acids, which are key factors that alter the membrane asymmetry of hepatocytes. This enabled us to figure out a feedback loop of bile acids and lipids across the cell membrane.
MeSH term(s)	Adenosine Triphosphatases/metabolism ; Bile Acids and Salts/metabolism ; Cell Membrane/metabolism ; Cholestasis, Intrahepatic/metabolism ; Humans ; Phospholipid Transfer Proteins/metabolism ; Phospholipids/metabolism
Chemical Substances	Bile Acids and Salts ; Phospholipid Transfer Proteins ; Phospholipids ; Adenosine Triphosphatases (EC 3.6.1.-) ; ATP8B1 protein, human (EC 3.6.1.3.)
Language	English
Publishing date	2022-03-29
Publishing country	United States
Document type	Journal Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2118656119
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1148: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito