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Article ; Online: Dynamic ion channel defies dogma.

Hellmich, Ute A

2023 Volume 621, Issue 7977, Page(s) 46–47

Language	English
Publishing date	2023-08-29
Publishing country	England
Document type	News
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/d41586-023-02486-9
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Article ; Online: TRP channels: branching out into the fungal kingdom.

Hellmich, Ute A / Delemotte, Lucie

Structure (London, England : 1993)

2022 Volume 30, Issue 1, Page(s) 2–4

Abstract: TRP channels have been heavily pursued as cryo-electron microscopy targets since they rang in the "resolution revolution." Although widespread in eukaryotes, a fungal TRP channel structure was missing. In this issue of Structure, Ahmed et al. (2022) ... ...

Abstract	TRP channels have been heavily pursued as cryo-electron microscopy targets since they rang in the "resolution revolution." Although widespread in eukaryotes, a fungal TRP channel structure was missing. In this issue of Structure, Ahmed et al. (2022) present structural insights into the regulation of yeast TRPY1 by Ca
MeSH term(s)	Cryoelectron Microscopy ; Saccharomyces cerevisiae
Language	English
Publishing date	2022-01-07
Publishing country	United States
Document type	Journal Article ; Comment
ZDB-ID	1213087-4
ISSN	1878-4186 ; 0969-2126
ISSN (online)	1878-4186
ISSN	0969-2126
DOI	10.1016/j.str.2021.12.006
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Article ; Online: What monomeric nucleotide binding domains can teach us about dimeric ABC proteins.

Ford, Robert C / Hellmich, Ute A

FEBS letters

2020 Volume 594, Issue 23, Page(s) 3857–3875

Abstract: The classic conceptualization of ATP binding cassette (ABC) transporter function is an ATP-dependent conformational change coupled to transport of a substrate across a biological membrane via the transmembrane domains (TMDs). The binding of two ATP ... ...

Abstract	The classic conceptualization of ATP binding cassette (ABC) transporter function is an ATP-dependent conformational change coupled to transport of a substrate across a biological membrane via the transmembrane domains (TMDs). The binding of two ATP molecules within the transporter's two nucleotide binding domains (NBDs) induces their dimerization. Despite retaining the ability to bind nucleotides, isolated NBDs frequently fail to dimerize. ABC proteins without a TMD, for example ABCE and ABCF, have NBDs tethered via elaborate linkers, further supporting that NBD dimerization does not readily occur for isolated NBDs. Intriguingly, even in full-length transporters, the NBD-dimerized, outward-facing state is not as frequently observed as might be expected. This leads to questions regarding what drives NBD interaction and the role of the TMDs or linkers. Understanding the NBD-nucleotide interaction and the subsequent NBD dimerization is thus pivotal for understanding ABC transporter activity in general. Here, we hope to provide new insights into ABC protein function by discussing the perplexing issue of (missing) NBD dimerization in isolation and in the context of full-length ABC proteins.
MeSH term(s)	ATP-Binding Cassette Transporters/chemistry ; ATP-Binding Cassette Transporters/metabolism ; Adenosine Triphosphate/metabolism ; Animals ; Binding Sites ; Humans ; Protein Binding ; Protein Domains ; Protein Multimerization
Chemical Substances	ATP-Binding Cassette Transporters ; Adenosine Triphosphate (8L70Q75FXE)
Language	English
Publishing date	2020-09-17
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1002/1873-3468.13921
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Article ; Online: Trapping of a Polyketide Synthase Module after C-C Bond Formation Reveals Transient Acyl Carrier Domain Interactions.

Dell, Maria / Tran, Mai Anh / Capper, Michael J / Sundaram, Srividhya / Fiedler, Jonas / Koehnke, Jesko / Hellmich, Ute A / Hertweck, Christian

Angewandte Chemie (International ed. in English)

2024 Volume 63, Issue 9, Page(s) e202315850

Abstract: Modular polyketide synthases (PKSs) are giant assembly lines that produce an impressive range of biologically active compounds. However, our understanding of the structural dynamics of these megasynthases, specifically the delivery of acyl carrier ... ...

Abstract	Modular polyketide synthases (PKSs) are giant assembly lines that produce an impressive range of biologically active compounds. However, our understanding of the structural dynamics of these megasynthases, specifically the delivery of acyl carrier protein (ACP)-bound building blocks to the catalytic site of the ketosynthase (KS) domain, remains severely limited. Using a multipronged structural approach, we report details of the inter-domain interactions after C-C bond formation in a chain-branching module of the rhizoxin PKS. Mechanism-based crosslinking of an engineered module was achieved using a synthetic substrate surrogate that serves as a Michael acceptor. The crosslinked protein allowed us to identify an asymmetric state of the dimeric protein complex upon C-C bond formation by cryo-electron microscopy (cryo-EM). The possible existence of two ACP binding sites, one of them a potential "parking position" for substrate loading, was also indicated by AlphaFold2 predictions. NMR spectroscopy showed that a transient complex is formed in solution, independent of the linker domains, and photochemical crosslinking/mass spectrometry of the standalone domains allowed us to pinpoint the interdomain interaction sites. The structural insights into a branching PKS module arrested after C-C bond formation allows a better understanding of domain dynamics and provides valuable information for the rational design of modular assembly lines.
MeSH term(s)	Polyketide Synthases/metabolism ; Cryoelectron Microscopy ; Binding Sites ; Catalytic Domain ; Acyl Carrier Protein/metabolism
Chemical Substances	Polyketide Synthases (79956-01-7) ; Acyl Carrier Protein
Language	English
Publishing date	2024-01-17
Publishing country	Germany
Document type	Journal Article
ZDB-ID	2011836-3
ISSN	1521-3773 ; 1433-7851
ISSN (online)	1521-3773
ISSN	1433-7851
DOI	10.1002/anie.202315850
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Article ; Online: Backbone NMR assignments of the extensive human and chicken TRPV4 N-terminal intrinsically disordered regions as important players in ion channel regulation.

Goretzki, Benedikt / Tebbe, Frederike / Mitrovic, Sarah-Ana / Hellmich, Ute A

Biomolecular NMR assignments

2022 Volume 16, Issue 2, Page(s) 205–212

Abstract: Transient receptor potential (TRP) channels are important pharmacological targets due to their ability to act as sensory transducers on the organismic and cellular level, as polymodal signal integrators and because of their role in numerous diseases. ... ...

Abstract	Transient receptor potential (TRP) channels are important pharmacological targets due to their ability to act as sensory transducers on the organismic and cellular level, as polymodal signal integrators and because of their role in numerous diseases. However, a detailed molecular understanding of the structural dynamics of TRP channels and their integration into larger cellular signalling networks remains challenging, in part due to the systematic absence of highly dynamic regions pivotal for channel regulation from available structures. In human TRP vanilloid 4 (TRPV4), a ubiquitously expressed homotetrameric cation channel involved in temperature, osmo- and mechano-sensation and in a multitude of (patho)physiological processes, the intrinsically disordered N-terminus encompasses 150 amino acids and thus represents > 17% of the entire channel sequence. Its deletion renders the channel significantly less excitable to agonists supporting a crucial role in TRPV4 activation and regulation. For a structural understanding and a comparison of its properties across species, we determined the NMR backbone assignments of the human and chicken TRPV4 N-terminal IDRs.
MeSH term(s)	Amino Acids ; Animals ; Chickens/metabolism ; Humans ; Magnetic Resonance Spectroscopy ; Nuclear Magnetic Resonance, Biomolecular ; TRPV Cation Channels/chemistry ; TRPV Cation Channels/metabolism
Chemical Substances	Amino Acids ; TRPV Cation Channels ; TRPV4 protein, human
Language	English
Publishing date	2022-04-22
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2388861-1
ISSN	1874-270X ; 1874-2718
ISSN (online)	1874-270X
ISSN	1874-2718
DOI	10.1007/s12104-022-10080-9
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Article: Functional Modulation of Chemical Mediators in Microbial Communities

Stallforth, Pierre / Mittag, Maria / Brakhage, Axel A. / Hertweck, Christian / Hellmich, Ute A.

Trends in biochemical sciences. 2022,

2022

Abstract: Interactions between microorganisms are often mediated by specialized metabolites. Whereas the structures and biosynthesis of these compounds may have been elucidated, microbes exist within complex microbiomes. Importantly, chemical signals can thus also ...

Abstract	Interactions between microorganisms are often mediated by specialized metabolites. Whereas the structures and biosynthesis of these compounds may have been elucidated, microbes exist within complex microbiomes. Importantly, chemical signals can thus also be subject to community-dependent modifications. Increasingly powerful chemical and biological tools allow to shed more light on this poorly understood aspect of chemical ecology. Here, we provide an overview over loss-of-function and gain-of-function chemical mediator modifications within microbial multipartner relationships. While loss-of-function modifications are abundant in the literature, only few gain-of-function modifications have been described despite their important role in microbial interactions. Research in this field holds great potential for our understanding of microbial interactions and may also provide novel tools for targeted interference with microbial signaling.
Keywords	biosynthesis ; chemical ecology ; gain-of-function mutation ; loss-of-function mutation ; metabolites ; microbiome
Language	English
Publishing place	Elsevier Ltd
Document type	Article
Note	Pre-press version
ZDB-ID	194220-7
ISSN	0968-0004 ; 0376-5067
ISSN	0968-0004 ; 0376-5067
DOI	10.1016/j.tibs.2022.07.006
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Article ; Online: The incredible diversity of structures and functions of ABC transporters.

Hamdoun, Amro / Hellmich, Ute A / Szakacs, Gergely / Kuchler, Karl

FEBS letters

2021 Volume 595, Issue 6, Page(s) 671–674

MeSH term(s)	ATP-Binding Cassette Transporters/chemistry ; Animals ; Humans ; Models, Molecular
Chemical Substances	ATP-Binding Cassette Transporters
Language	English
Publishing date	2021-03-19
Publishing country	England
Document type	Editorial
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1002/1873-3468.14061
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Article: Functional modulation of chemical mediators in microbial communities.

Stallforth, Pierre / Mittag, Maria / Brakhage, Axel A / Hertweck, Christian / Hellmich, Ute A

Trends in biochemical sciences

2022 Volume 48, Issue 1, Page(s) 71–81

Abstract: Interactions between microorganisms are often mediated by specialized metabolites. Although the structures and biosynthesis of these compounds may have been elucidated, microbes exist within complex microbiomes and chemical signals can thus also be ... ...

Abstract	Interactions between microorganisms are often mediated by specialized metabolites. Although the structures and biosynthesis of these compounds may have been elucidated, microbes exist within complex microbiomes and chemical signals can thus also be subject to community-dependent modifications. Increasingly powerful chemical and biological tools allow to shed light on this poorly understood aspect of chemical ecology. We provide an overview of loss-of-function and gain-of-function chemical mediator (CM) modifications within microbial multipartner relationships. Although loss-of-function modifications are abundant in the literature, few gain-of-function modifications have been described despite their important role in microbial interactions. Research in this field holds great potential for our understanding of microbial interactions and may also provide novel tools for targeted interference with microbial signaling.
MeSH term(s)	Microbiota
Language	English
Publishing date	2022-08-16
Publishing country	England
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	194216-5
ISSN	1362-4326 ; 0968-0004 ; 0376-5067
ISSN (online)	1362-4326
ISSN	0968-0004 ; 0376-5067
DOI	10.1016/j.tibs.2022.07.006
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Article ; Online: Extent of intrinsic disorder and NMR chemical shift assignments of the distal N-termini from human TRPV1, TRPV2 and TRPV3 ion channels.

Wiedemann, Christoph / Goretzki, Benedikt / Merz, Zoe N / Tebbe, Frederike / Schmitt, Pauline / Hellmich, Ute A

Biomolecular NMR assignments

2022 Volume 16, Issue 2, Page(s) 289–296

Abstract: The mammalian Transient Receptor Potential Vanilloid (TRPV) channels are a family of six tetrameric ion channels localized at the plasma membrane. The group I members of the family, TRPV1 through TRPV4, are heat-activated and exhibit remarkable ... ...

Abstract	The mammalian Transient Receptor Potential Vanilloid (TRPV) channels are a family of six tetrameric ion channels localized at the plasma membrane. The group I members of the family, TRPV1 through TRPV4, are heat-activated and exhibit remarkable polymodality. The distal N-termini of group I TRPV channels contain large intrinsically disordered regions (IDRs), ranging from ~ 75 amino acids (TRPV2) to ~ 150 amino acids (TRPV4), the vast majority of which is invisible in the structural models published so far. These IDRs provide important binding sites for cytosolic partners, and their deletion is detrimental to channel activity and regulation. Recently, we reported the NMR backbone assignments of the distal TRPV4 N-terminus and noticed some discrepancies between the extent of disorder predicted solely based on protein sequence and from experimentally determined chemical shifts. Thus, for an analysis of the extent of disorder in the distal N-termini of all group I TRPV channels, we now report the NMR assignments for the human TRPV1, TRPV2 and TRPV3 IDRs.
MeSH term(s)	Amino Acid Sequence ; Amino Acids ; Animals ; Hot Temperature ; Humans ; Mammals/metabolism ; Nuclear Magnetic Resonance, Biomolecular ; TRPV Cation Channels/chemistry ; TRPV Cation Channels/metabolism
Chemical Substances	Amino Acids ; TRPV Cation Channels ; TRPV1 protein, human ; TRPV2 protein, human ; TRPV3 protein, human
Language	English
Publishing date	2022-06-06
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2388861-1
ISSN	1874-270X ; 1874-2718
ISSN (online)	1874-270X
ISSN	1874-2718
DOI	10.1007/s12104-022-10093-4
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Article ; Online: Backbone NMR assignment of the nucleotide binding domain of the Bacillus subtilis ABC multidrug transporter BmrA in the post-hydrolysis state.

Pérez Carrillo, Victor Hugo / Rose-Sperling, Dania / Tran, Mai Anh / Wiedemann, Christoph / Hellmich, Ute A

Biomolecular NMR assignments

2022 Volume 16, Issue 1, Page(s) 81–86

Abstract: ATP binding cassette (ABC) proteins are present in all phyla of life and form one of the largest protein families. The Bacillus subtilis ABC transporter BmrA is a functional homodimer that can extrude many different harmful compounds out of the cell. ... ...

Abstract	ATP binding cassette (ABC) proteins are present in all phyla of life and form one of the largest protein families. The Bacillus subtilis ABC transporter BmrA is a functional homodimer that can extrude many different harmful compounds out of the cell. Each BmrA monomer is composed of a transmembrane domain (TMD) and a nucleotide binding domain (NBD). While the TMDs of ABC transporters are sequentially diverse, the highly conserved NBDs harbor distinctive conserved motifs that enable nucleotide binding and hydrolysis, interdomain communication and that mark a protein as a member of the ABC superfamily. In the catalytic cycle of an ABC transporter, the NBDs function as the molecular motor that fuels substrate translocation across the membrane via the TMDs and are thus pivotal for the entire transport process. For a better understanding of the structural and dynamic consequences of nucleotide interactions within the NBD at atomic resolution, we determined the
MeSH term(s)	ATP-Binding Cassette Transporters ; Bacillus/metabolism ; Bacillus subtilis/metabolism ; Hydrolysis ; Nuclear Magnetic Resonance, Biomolecular ; Nucleotides/metabolism
Chemical Substances	ATP-Binding Cassette Transporters ; Nucleotides
Language	English
Publishing date	2022-01-05
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2388861-1
ISSN	1874-270X ; 1874-2718
ISSN (online)	1874-270X
ISSN	1874-2718
DOI	10.1007/s12104-021-10063-2
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