5lp5: Difference between revisions
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<StructureSection load='5lp5' size='340' side='right'caption='[[5lp5]], [[Resolution|resolution]] 2.74Å' scene=''> | <StructureSection load='5lp5' size='340' side='right'caption='[[5lp5]], [[Resolution|resolution]] 2.74Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5lp5]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LP5 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5lp5]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LP5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LP5 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.74Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5lp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lp5 OCA], [https://pdbe.org/5lp5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lp5 RCSB], [https://www.ebi.ac.uk/pdbsum/5lp5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lp5 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/O25924_HELPY O25924_HELPY] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Helicobacter pylori 26695]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Boneca | [[Category: Boneca IG]] | ||
[[Category: Contreras-Martel | [[Category: Contreras-Martel C]] | ||
[[Category: Dessen | [[Category: Dessen A]] | ||
[[Category: Ecobichon | [[Category: Ecobichon C]] | ||
[[Category: Ghachi | [[Category: El Ghachi M]] | ||
[[Category: Hardouin | [[Category: Hardouin P]] | ||
[[Category: Hicham | [[Category: Hicham S]] | ||
[[Category: Maragno | [[Category: Maragno DM]] | ||
[[Category: Martins | [[Category: Martins A]] | ||
[[Category: Mattei | [[Category: Mattei PJ]] | ||
Latest revision as of 21:38, 18 October 2023
Complex between Penicillin-Binding Protein (PBP2) and MreC from Helicobacter pyloriComplex between Penicillin-Binding Protein (PBP2) and MreC from Helicobacter pylori
Structural highlights
FunctionPublication Abstract from PubMedBacterial cell wall biosynthesis is an essential process that requires the coordinated activity of peptidoglycan biosynthesis enzymes within multi-protein complexes involved in cell division (the "divisome") and lateral wall growth (the "elongasome"). MreC is a structural protein that serves as a platform during wall elongation, scaffolding other essential peptidoglycan biosynthesis macromolecules, such as penicillin-binding proteins. Despite the importance of these multi-partite complexes, details of their architecture have remained elusive due to the transitory nature of their interactions. Here, we present the crystal structures of the soluble PBP2:MreC core elongasome complex from Helicobacter pylori, and of uncomplexed PBP2. PBP2 recognizes the two-winged MreC molecule upon opening of its N-terminal region, revealing a hydrophobic zipper that serves as binding platform. The PBP2:MreC interface is essential both for protein recognition in vitro and maintenance of bacterial shape and growth. This work allows visualization as to how peptidoglycan machinery proteins are scaffolded, revealing interaction regions that could be targeted by tailored inhibitors.Bacterial wall biosynthesis is a complex process that requires the coordination of multiple enzymes. Here, the authors structurally characterize the PBP2:MreC complex involved in peptidoglycan elongation and cross-linking, and demonstrate that its disruption leads to loss of H. pylori shape and inability to sustain growth. Molecular architecture of the PBP2-MreC core bacterial cell wall synthesis complex.,Contreras-Martel C, Martins A, Ecobichon C, Trindade DM, Mattei PJ, Hicham S, Hardouin P, Ghachi ME, Boneca IG, Dessen A Nat Commun. 2017 Oct 3;8(1):776. doi: 10.1038/s41467-017-00783-2. PMID:28974686[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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