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  1. Article ; Online: Determining the helical tilt angle and dynamic properties of the transmembrane domains of pinholin S

    Khan, Rasal H / Ahammad, Tanbir / Sahu, Indra D / Rotich, Nancy C / Daufel, Andrew / Lorigan, Gary A

    Biochimica et biophysica acta. Biomembranes

    2023  Volume 1865, Issue 5, Page(s) 184154

    Abstract: The lytic cycle of bacteriophage φ21 for the infected E. coli is initiated by pinholin ... ...

    Abstract The lytic cycle of bacteriophage φ21 for the infected E. coli is initiated by pinholin S
    MeSH term(s) Electron Spin Resonance Spectroscopy ; Lipid Bilayers/chemistry ; Escherichia coli/metabolism ; Amino Acid Sequence ; Spin Labels
    Chemical Substances Lipid Bilayers ; Spin Labels
    Language English
    Publishing date 2023-04-05
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 60-7
    ISSN 1879-2642 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2642 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbamem.2023.184154
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Probing the Structural Topology and Dynamic Properties of gp28 Using Continuous Wave Electron Paramagnetic Resonance Spectroscopy.

    Khan, Rasal H / Rotich, Nancy C / Morris, Andrew / Ahammad, Tanbir / Baral, Binaya / Sahu, Indra D / Lorigan, Gary A

    The journal of physical chemistry. B

    2023  Volume 127, Issue 43, Page(s) 9236–9247

    Abstract: Lysis of Gram-negative bacteria by dsDNA phages is accomplished through either the canonical holin-endolysin pathway or the pinholin-SAR endolysin pathway. During lysis, the outer membrane (OM) is disrupted, typically by two-component spanins or ... ...

    Abstract Lysis of Gram-negative bacteria by dsDNA phages is accomplished through either the canonical holin-endolysin pathway or the pinholin-SAR endolysin pathway. During lysis, the outer membrane (OM) is disrupted, typically by two-component spanins or unimolecular spanins. However, in the absence of spanins, phages use alternative proteins called Disruptin to disrupt the OM. The Disruptin family includes the cationic antimicrobial peptide gp28, which is found in the virulent podophage φKT. In this study, EPR spectroscopy was used to analyze the dynamics and topology of gp28 incorporated into a lipid bilayer, revealing differences in mobility, depth parameter, and membrane interaction among different segments and residues of the protein. Our results indicate that multiple points of helix 2 and helix 3 interact with the phospholipid membrane, while others are solvent-exposed, suggesting that gp28 is a surface-bound peptide. The CW-EPR power saturation data and helical wheel analysis confirmed the amphipathic-helical structure of gp28. Additionally, course-grain molecular dynamics simulations were further used to develop the structural model of the gp28 peptide associated with the lipid bilayers. Based on the data obtained in this study, we propose a structural topology model for gp28 with respect to the membrane. This work provides important insights into the structural and dynamic properties of gp28 incorporated into a lipid bilayer environment.
    MeSH term(s) Lipid Bilayers/chemistry ; Electron Spin Resonance Spectroscopy ; Bacteriophages/metabolism ; Gram-Negative Bacteria/metabolism ; Antimicrobial Cationic Peptides/metabolism
    Chemical Substances Lipid Bilayers ; Antimicrobial Cationic Peptides
    Language English
    Publishing date 2023-10-19
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ISSN 1520-5207
    ISSN (online) 1520-5207
    DOI 10.1021/acs.jpcb.3c03679
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Structural Dynamics and Topology of the Inactive Form of S²¹ Holin in a Lipid Bilayer Using Continuous-Wave Electron Paramagnetic Resonance Spectroscopy

    Ahammad, Tanbir / Drew, Daniel L / Khan, Rasal H / Sahu, Indra D / Faul, Emily / Li, Tianyan / Lorigan, Gary A

    Journal of physical chemistry. 2020 June 05, v. 124, no. 26

    2020  

    Abstract: The bacteriophage infection cycle plays a crucial role in recycling the world’s biomass. Bacteriophages devise various cell lysis systems to strictly control the length of the infection cycle for an efficient phage life cycle. Phages evolved with lysis ... ...

    Abstract The bacteriophage infection cycle plays a crucial role in recycling the world’s biomass. Bacteriophages devise various cell lysis systems to strictly control the length of the infection cycle for an efficient phage life cycle. Phages evolved with lysis protein systems, which can control and fine-tune the length of this infection cycle depending on the host and growing environment. Among these lysis proteins, holin controls the first and rate-limiting step of host cell lysis by permeabilizing the inner membrane at an allele-specific time and concentration hence known as the simplest molecular clock. Pinholin S²¹ is the holin from phage Φ21, which defines the cell lysis time through a predefined ratio of active pinholin and antipinholin (inactive form of pinholin). Active pinholin and antipinholin fine-tune the lysis timing through structural dynamics and conformational changes. Previously we reported the structural dynamics and topology of active pinholin S²¹68. Currently, there is no detailed structural study of the antipinholin using biophysical techniques. In this study, the structural dynamics and topology of antipinholin S²¹68IRS in DMPC proteoliposomes is investigated using electron paramagnetic resonance (EPR) spectroscopic techniques. Continuous-wave (CW) EPR line shape analysis experiments of 35 different R1 side chains of S²¹68IRS indicated restricted mobility of the transmembrane domains (TMDs), which were predicted to be inside the lipid bilayer when compared to the N- and C-termini R1 side chains. In addition, the R1 accessibility test performed on 24 residues using the CW-EPR power saturation experiment indicated that TMD1 and TMD2 of S²¹68IRS were incorporated into the lipid bilayer where N- and C-termini were located outside of the lipid bilayer. Based on this study, a tentative model of S²¹68IRS is proposed where both TMDs remain incorporated into the lipid bilayer and N- and C-termini are located outside of the lipid bilayer. This work will pave the way for the further studies of other holins using biophysical techniques and will give structural insights into these biological clocks in molecular detail.
    Keywords bacteriophages ; biomass ; electron paramagnetic resonance spectroscopy ; lipid bilayers ; models ; phylogeny ; physical chemistry ; reaction kinetics ; topology
    Language English
    Dates of publication 2020-0605
    Size p. 5370-5379.
    Publishing place American Chemical Society
    Document type Article
    Note NAL-AP-2-clean
    ISSN 1520-5207
    DOI 10.1021/acs.jpcb.0c03575
    Database NAL-Catalogue (AGRICOLA)

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  4. Article ; Online: Probing the local secondary structure of bacteriophage S

    Drew, Daniel L / Ahammad, Tanbir / Serafin, Rachel A / Sahu, Indra D / Khan, Rasal H / Faul, Emily / McCarrick, Robert M / Lorigan, Gary A

    Biochimica et biophysica acta. Biomembranes

    2021  Volume 1864, Issue 3, Page(s) 183836

    Abstract: There have recently been advances in methods for detecting local secondary structures of membrane protein using electron paramagnetic resonance (EPR). A three pulsed electron spin echo envelope modulation (ESEEM) approach was used to determine the local ... ...

    Abstract There have recently been advances in methods for detecting local secondary structures of membrane protein using electron paramagnetic resonance (EPR). A three pulsed electron spin echo envelope modulation (ESEEM) approach was used to determine the local helical secondary structure of the small hole forming membrane protein, S
    MeSH term(s) Amino Acid Sequence ; Bacteriophages/metabolism ; Electron Spin Resonance Spectroscopy/methods ; Lipid Bilayers/chemistry ; Membrane Proteins/chemistry ; Protein Structure, Secondary ; Viral Proteins/chemistry
    Chemical Substances Lipid Bilayers ; Membrane Proteins ; Viral Proteins
    Language English
    Publishing date 2021-12-11
    Publishing country Netherlands
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 60-7
    ISSN 1879-2642 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2642 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbamem.2021.183836
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.247: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
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  5. Article ; Online: Pinholin S

    Ahammad, Tanbir / Khan, Rasal H / Sahu, Indra D / Drew, Daniel L / Faul, Emily / Li, Tianyan / McCarrick, Robert M / Lorigan, Gary A

    Biochimica et biophysica acta. Biomembranes

    2021  Volume 1863, Issue 12, Page(s) 183771

    Abstract: The bacteriophage infection cycle is terminated at a predefined time to release the progeny virions via a robust lytic system composed of holin, endolysin, and spanin proteins. Holin is the timekeeper of this process. Pinholin ... ...

    Abstract The bacteriophage infection cycle is terminated at a predefined time to release the progeny virions via a robust lytic system composed of holin, endolysin, and spanin proteins. Holin is the timekeeper of this process. Pinholin S
    MeSH term(s) Bacteriophages/chemistry ; Bacteriophages/genetics ; Biological Transport ; Cell Death/genetics ; Endopeptidases/chemistry ; Endopeptidases/genetics ; Membrane Proteins/chemistry ; Membrane Proteins/genetics ; Mutation/genetics ; Viral Proteins/chemistry ; Viral Proteins/genetics ; Virion/chemistry ; Virion/genetics
    Chemical Substances Membrane Proteins ; Viral Proteins ; pinholin S(21) protein, phage phi21 ; Endopeptidases (EC 3.4.-) ; endolysin (EC 3.4.99.-)
    Language English
    Publishing date 2021-09-07
    Publishing country Netherlands
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 60-7
    ISSN 1879-2642 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2642 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbamem.2021.183771
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.247: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  6. Article ; Online: Structural Dynamics and Topology of the Inactive Form of S

    Ahammad, Tanbir / Drew, Daniel L / Khan, Rasal H / Sahu, Indra D / Faul, Emily / Li, Tianyan / Lorigan, Gary A

    The journal of physical chemistry. B

    2020  Volume 124, Issue 26, Page(s) 5370–5379

    Abstract: The bacteriophage infection cycle plays a crucial role in recycling the world's biomass. Bacteriophages devise various cell lysis systems to strictly control the length of the infection cycle for an efficient phage life cycle. Phages evolved with lysis ... ...

    Abstract The bacteriophage infection cycle plays a crucial role in recycling the world's biomass. Bacteriophages devise various cell lysis systems to strictly control the length of the infection cycle for an efficient phage life cycle. Phages evolved with lysis protein systems, which can control and fine-tune the length of this infection cycle depending on the host and growing environment. Among these lysis proteins, holin controls the first and rate-limiting step of host cell lysis by permeabilizing the inner membrane at an allele-specific time and concentration hence known as the simplest molecular clock. Pinholin S
    MeSH term(s) Bacteriophages/genetics ; Electron Spin Resonance Spectroscopy ; Lipid Bilayers ; Viral Proteins
    Chemical Substances Lipid Bilayers ; Viral Proteins
    Language English
    Publishing date 2020-06-19
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ISSN 1520-5207
    ISSN (online) 1520-5207
    DOI 10.1021/acs.jpcb.0c03575
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Conformational Differences Are Observed for the Active and Inactive Forms of Pinholin S

    Ahammad, Tanbir / Drew, Daniel L / Sahu, Indra D / Khan, Rasal H / Butcher, Brandon J / Serafin, Rachel A / Galende, Alberto P / McCarrick, Robert M / Lorigan, Gary A

    The journal of physical chemistry. B

    2020  Volume 124, Issue 50, Page(s) 11396–11405

    Abstract: Bacteriophages have evolved with an efficient host cell lysis mechanism to terminate the infection cycle and release the new progeny virions at the optimum time, allowing adaptation with the changing host and environment. Among the lytic proteins, holin ... ...

    Abstract Bacteriophages have evolved with an efficient host cell lysis mechanism to terminate the infection cycle and release the new progeny virions at the optimum time, allowing adaptation with the changing host and environment. Among the lytic proteins, holin controls the first and rate-limiting step of host cell lysis by permeabilizing the inner membrane at an allele-specific time known as "holin triggering". Pinholin S
    MeSH term(s) Bacteriophages ; Cell Wall ; Electron Spin Resonance Spectroscopy ; Lipid Bilayers ; Viral Proteins
    Chemical Substances Lipid Bilayers ; Viral Proteins
    Language English
    Publishing date 2020-12-08
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ISSN 1520-5207
    ISSN (online) 1520-5207
    DOI 10.1021/acs.jpcb.0c09081
    Database MEDical Literature Analysis and Retrieval System OnLINE

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