View source for 5hxd


==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 with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5HXD 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]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=5hxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hxd OCA], [https://pdbe.org/5hxd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hxd RCSB], [https://www.ebi.ac.uk/pdbsum/5hxd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hxd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MPAA_ECO57 MPAA_ECO57] 
<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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5hxd" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli O157:H7]]
[[Category: Large Structures]]
[[Category: Bai G]]
[[Category: Kang X]]
[[Category: Li Z]]
[[Category: Liu X]]
[[Category: Ma Y]]
[[Category: Mu S]]
[[Category: Yuan Z]]
[[Category: Zhang X]]
[[Category: Zhao J]]