4ox5: Difference between revisions
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<StructureSection load='4ox5' size='340' side='right'caption='[[4ox5]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='4ox5' size='340' side='right'caption='[[4ox5]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ox5]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ox5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_R6 Streptococcus pneumoniae R6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OX5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OX5 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4ox5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ox5 OCA], [https://pdbe.org/4ox5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ox5 RCSB], [https://www.ebi.ac.uk/pdbsum/4ox5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ox5 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8DQQ1_STRR6 Q8DQQ1_STRR6] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Streptococcus pneumoniae R6]] | ||
[[Category: Aldridge | [[Category: Aldridge C]] | ||
[[Category: Cleverley | [[Category: Cleverley RM]] | ||
[[Category: Daniel | [[Category: Daniel RA]] | ||
[[Category: Duchene | [[Category: Duchene MC]] | ||
[[Category: Hoyland | [[Category: Hoyland CN]] | ||
[[Category: Lewis | [[Category: Lewis RJ]] | ||
[[Category: Sidiq | [[Category: Sidiq K]] | ||
[[Category: Vollmer | [[Category: Vollmer W]] | ||
Revision as of 15:30, 1 February 2023
Structure of the LdcB LD-carboxypeptidase reveals the molecular basis of peptidoglycan recognitionStructure of the LdcB LD-carboxypeptidase reveals the molecular basis of peptidoglycan recognition
Structural highlights
FunctionPublication Abstract from PubMedPeptidoglycan surrounds the bacterial cytoplasmic membrane to protect the cell against osmolysis. The biosynthesis of peptidoglycan, made of glycan strands crosslinked by short peptides, is the target of antibiotics like beta-lactams and glycopeptides. Nascent peptidoglycan contains pentapeptides that are trimmed by carboxypeptidases to tetra- and tripeptides. The well-characterized DD-carboxypeptidases hydrolyze the terminal D-alanine from the stem pentapeptide to produce a tetrapeptide. However, few LD-carboxypeptidases that produce tripeptides have been identified, and nothing is known about substrate specificity in these enzymes. We report biochemical properties and crystal structures of the LD-carboxypeptidases LdcB from Streptococcus pneumoniae, Bacillus anthracis, and Bacillus subtilis. The enzymes are active against bacterial cell wall tetrapeptides and adopt a zinc-carboxypeptidase fold characteristic of the LAS superfamily. We have also solved the structure of S. pneumoniae LdcB with a product mimic, elucidating the residues essential for peptidoglycan recognition and the conformational changes that occur on ligand binding. Structure of the LdcB LD-Carboxypeptidase Reveals the Molecular Basis of Peptidoglycan Recognition.,Hoyland CN, Aldridge C, Cleverley RM, Duchene MC, Minasov G, Onopriyenko O, Sidiq K, Stogios PJ, Anderson WF, Daniel RA, Savchenko A, Vollmer W, Lewis RJ Structure. 2014 Jun 4. pii: S0969-2126(14)00139-7. doi:, 10.1016/j.str.2014.04.015. PMID:24909784[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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