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'''Unreleased structure'''


The entry 5hxd is ON HOLD  until Paper Publication
==Crystal structure of murein-tripeptide amidase MpaA from Escherichia coli O157==
<StructureSection load='5hxd' size='340' side='right' caption='[[5hxd]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5hxd]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HXD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HXD FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5hxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hxd OCA], [http://pdbe.org/5hxd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hxd RCSB], [http://www.ebi.ac.uk/pdbsum/5hxd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hxd ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Peptidoglycan (PG) is an essential component of the cell wall, and undergoes reconstruction by various PG hydrolases during cell growth, development and division. The murein- tripeptide (Mtp) amidase MpaA belongs to PG hydrolase family and is responsible for cleaving the gamma-D-Glu-meso-Dap amide bond in the Mtp released during PG turnover. The current paper reports the crystal structure of MpaA from Escherichia coli (E. coli) O157 at 2.6 A resolution. The asymmetric unit consists of two protein molecules and each monomer represents the common alpha/beta fold of metallo-carboxypeptidases (MCP). The Tyr133-Asp143 loop appears to mediate the entrance and binding of the substrate into the active groove. A structural comparison of MpaA with its homologue from Vibrio harveyi showed that MpaA has narrower active pocket entrance with a smaller surface opening, which is determined by the Val204-Thr211 loop. The reported structure provides a starting point for the molecular mechanism of MpaA in a significant human pathogen.


Authors: Ma, Y., Bai, G., Zhang, X., Zhao, J., Yuan, Z., Kang, X., Li, Z., Mu, S., Liu, X.
Crystal Structure of Murein-Tripeptide Amidase MpaA from Escherichia coli O157 at 2.6 A Resolution.,Ma Y, Bai G, Cui Y, Zhao J, Yuan Z, Liu X Protein Pept Lett. 2016 Nov 28. PMID:27894248<ref>PMID:27894248</ref>


Description: Crystal structure of murein-tripeptide amidase MpaA from Escherichia coli O157
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5hxd" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bai, G]]
[[Category: Bai, G]]
[[Category: Zhang, X]]
[[Category: Kang, X]]
[[Category: Mu, S]]
[[Category: Li, Z]]
[[Category: Liu, X]]
[[Category: Liu, X]]
[[Category: Ma, Y]]
[[Category: Ma, Y]]
[[Category: Mu, S]]
[[Category: Yuan, Z]]
[[Category: Zhang, X]]
[[Category: Zhao, J]]
[[Category: Zhao, J]]
[[Category: Li, Z]]
[[Category: Escherichia coli o157]]
[[Category: Yuan, Z]]
[[Category: Hydrolase]]
[[Category: Kang, X]]
[[Category: Mpaa]]
[[Category: Murein-tripeptide amidase]]
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