4jid: Difference between revisions
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==Crystal structure of BaLdcB / VanY-like L,D-carboxypeptidase Zinc(II)-free== | ==Crystal structure of BaLdcB / VanY-like L,D-carboxypeptidase Zinc(II)-free== | ||
<StructureSection load='4jid' size='340' side='right' caption='[[4jid]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='4jid' size='340' side='right'caption='[[4jid]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4jid]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4jid]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis_str._Ames Bacillus anthracis str. Ames]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JID OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JID 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 | </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></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=4jid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jid OCA], [https://pdbe.org/4jid PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jid RCSB], [https://www.ebi.ac.uk/pdbsum/4jid PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jid 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/A0A6L8PDI9_BACAN A0A6L8PDI9_BACAN] | |||
<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: | [[Category: Bacillus anthracis str. Ames]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Anderson WF]] | ||
[[Category: Minasov | [[Category: Minasov G]] | ||
[[Category: Onopriyenko | [[Category: Onopriyenko O]] | ||
[[Category: Peterson | [[Category: Peterson SN]] | ||
[[Category: Savchenko | [[Category: Savchenko A]] | ||
[[Category: Shatsman | [[Category: Shatsman S]] | ||
[[Category: Skarina | [[Category: Skarina T]] | ||
[[Category: Wawrzak | [[Category: Wawrzak Z]] | ||
Revision as of 14:14, 24 November 2022
Crystal structure of BaLdcB / VanY-like L,D-carboxypeptidase Zinc(II)-freeCrystal structure of BaLdcB / VanY-like L,D-carboxypeptidase Zinc(II)-free
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. References
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