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  1. Article: The Pneumococcal Divisome: Dynamic Control of

    Briggs, Nicholas S / Bruce, Kevin E / Naskar, Souvik / Winkler, Malcolm E / Roper, David I

    Frontiers in microbiology

    2021  Volume 12, Page(s) 737396

    Abstract: Cell division ... ...

    Abstract Cell division in
    Language English
    Publishing date 2021-10-18
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2587354-4
    ISSN 1664-302X
    ISSN 1664-302X
    DOI 10.3389/fmicb.2021.737396
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Structural basis of peptidoglycan synthesis by E. coli RodA-PBP2 complex.

    Nygaard, Rie / Graham, Chris L B / Belcher Dufrisne, Meagan / Colburn, Jonathan D / Pepe, Joseph / Hydorn, Molly A / Corradi, Silvia / Brown, Chelsea M / Ashraf, Khuram U / Vickery, Owen N / Briggs, Nicholas S / Deering, John J / Kloss, Brian / Botta, Bruno / Clarke, Oliver B / Columbus, Linda / Dworkin, Jonathan / Stansfeld, Phillip J / Roper, David I /
    Mancia, Filippo

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 5151

    Abstract: Peptidoglycan (PG) is an essential structural component of the bacterial cell wall that is synthetized during cell division and elongation. PG forms an extracellular polymer crucial for cellular viability, the synthesis of which is the target of many ... ...

    Abstract Peptidoglycan (PG) is an essential structural component of the bacterial cell wall that is synthetized during cell division and elongation. PG forms an extracellular polymer crucial for cellular viability, the synthesis of which is the target of many antibiotics. PG assembly requires a glycosyltransferase (GT) to generate a glycan polymer using a Lipid II substrate, which is then crosslinked to the existing PG via a transpeptidase (TP) reaction. A Shape, Elongation, Division and Sporulation (SEDS) GT enzyme and a Class B Penicillin Binding Protein (PBP) form the core of the multi-protein complex required for PG assembly. Here we used single particle cryo-electron microscopy to determine the structure of a cell elongation-specific E. coli RodA-PBP2 complex. We combine this information with biochemical, genetic, spectroscopic, and computational analyses to identify the Lipid II binding sites and propose a mechanism for Lipid II polymerization. Our data suggest a hypothesis for the movement of the glycan strand from the Lipid II polymerization site of RodA towards the TP site of PBP2, functionally linking these two central enzymatic activities required for cell wall peptidoglycan biosynthesis.
    MeSH term(s) Cryoelectron Microscopy ; Escherichia coli/genetics ; Peptidoglycan ; Molecular Biology ; Anti-Bacterial Agents ; Glycosyltransferases ; Peptidyl Transferases
    Chemical Substances Peptidoglycan ; Anti-Bacterial Agents ; Glycosyltransferases (EC 2.4.-) ; Peptidyl Transferases (EC 2.3.2.12)
    Language English
    Publishing date 2023-08-24
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-40483-8
    Database MEDical Literature Analysis and Retrieval System OnLINE

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