View source for 5opz


==Crystal structure of Serratia marcescens L-Ala D-Glu endopeptidase ChiX==
<StructureSection load='5opz' size='340' side='right'caption='[[5opz]], [[Resolution|resolution]] 1.34&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5opz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OPZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OPZ 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]] 1.34&#8491;</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=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=5opz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5opz OCA], [https://pdbe.org/5opz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5opz RCSB], [https://www.ebi.ac.uk/pdbsum/5opz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5opz ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Gram-negative bacterium Serratia marcescens secretes a number of proteins that are involved in extracellular chitin degradation. This so-called chitinolytic machinery includes three types of chitinase enzymes and a lytic polysaccharide monooxygenase. An operon has been identified in S. marcescens , chiWXYZ , that is thought to be involved in the secretion of the chitinolytic machinery. Genetic evidence points to the ChiX protein being a key player in the secretion mechanism, since deletion of the chiX gene in S. marcescens led to a mutant strain blocked for secretion of all members of the chitinolytic machinery. In this work, a detailed structural and biochemical characterisation of ChiX is presented. The high resolution crystal structure of ChiX reveals the protein to be a member of the LAS family of peptidases. ChiX is shown to be a Zinc-containing metalloenzyme and in vitro assays demonstrate ChiX is an L-Ala D-Glu endopeptidase that cleaves the crosslinks in bacterial peptidoglycan. This catalytic activity is shown to be intimately linked with the secretion of the chitinolytic machinery, since substitution of the ChiX Asp-120 residue results in a variant protein that is both unable to digest peptidoglycan and cannot rescue the phenoytype of a chiX mutant strain.

Structure and activity of ChiX, a peptidoglycan hydrolase required for chitinase secretion by Serratia marcescens .,Owen RA, Fyfe PK, Lodge A, Biboy J, Vollmer W, Hunter WN, Sargent F Biochem J. 2017 Dec 11. pii: BCJ20170633. doi: 10.1042/BCJ20170633. PMID:29229757<ref>PMID:29229757</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5opz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Serratia marcescens]]
[[Category: Biboy J]]
[[Category: Fyfe PK]]
[[Category: Hunter WN]]
[[Category: Lodge A]]
[[Category: Owen RA]]
[[Category: Sargent F]]
[[Category: Vollmer W]]