View source for 4wcn


==Crystal Structure of Tripeptide bound Cell Shape Determinant Csd4 protein from Helicobacter pylori==
<StructureSection load='4wcn' size='340' side='right'caption='[[4wcn]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4wcn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_G27 Helicobacter pylori G27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WCN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WCN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3KS:N-ACETYL-L-ALANYL-N-[(1S,5R)-5-AMINO-1,5-DICARBOXYPENTYL]-D-GLUTAMINE'>3KS</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=4wcn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wcn OCA], [https://pdbe.org/4wcn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wcn RCSB], [https://www.ebi.ac.uk/pdbsum/4wcn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wcn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B5ZAD9_HELPG B5ZAD9_HELPG] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Peptidoglycan (PG) modifying carboxypeptidases (CPs) are important determinants of bacterial cell shape. Here, we report crystal structures of Csd4, a three-domain protein from the human gastric pathogen Helicobacter pylori. The catalytic zinc in Csd4 is coordinated by a rare H+E+Q configuration that is conserved amongst most Csd4 homologs, which form a distinct subfamily of CPs. Substitution of the glutamine to histidine, the residue found in prototypical zinc carboxypeptidases, resulted in decreased enzyme activity and inhibition by phosphate. Expression of the histidine variant at the native locus in a H. pylori csd4 deletion strain did not restore the wild-type helical morphology. Biochemical assays show that Csd4 can cleave a tripeptide PG substrate analog to release m-DAP. Structures of Csd4 with this substrate analog or product bound at the active site reveal determinants of peptidoglycan specificity and the mechanism to cleave an isopeptide bond to release m-DAP. Our data suggest that Csd4 is the archetype of a new CP subfamily with a domain scheme that differs from this large family of peptide cleaving enzymes.

Helical Shape of Helicobacter pylori Requires an Atypical Glutamine as a Zinc Ligand in the Carboxypeptidase Csd4.,Chan AC, Blair KM, Liu Y, Frirdich E, Gaynor EC, Tanner ME, Salama NR, Murphy ME J Biol Chem. 2014 Dec 12. pii: jbc.M114.624734. PMID:25505267<ref>PMID:25505267</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4wcn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Helicobacter pylori G27]]
[[Category: Large Structures]]
[[Category: Chan AC]]
[[Category: Murphy ME]]