1tzp

<table><tr><td colspan='2'>[[1tzp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TZP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1TZP FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BU1:1,4-BUTANEDIOL'>BU1</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1u10|1u10]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mepA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1tzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tzp OCA], [http://pdbe.org/1tzp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tzp RCSB], [http://www.ebi.ac.uk/pdbsum/1tzp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tzp ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/MEPA_ECOLI MEPA_ECOLI]] Involved in the removal of murein from the sacculus. May also facilitate integration of nascent murein strands into the sacculus by cleaving the peptide bonds between neighboring strands in mature murein.<ref>PMID:15292190</ref>

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== Publication Abstract from PubMed ==

LAS enzymes are a group of metallopeptidases that share an active site architecture and a core folding motif and have been named according to the group members lysostaphin, D-Ala-D-Ala carboxypeptidase and sonic hedgehog. Escherichia coli MepA is a periplasmic, penicillin-insensitive murein endopeptidase that cleaves the D-alanyl-meso-2,6-diamino-pimelyl amide bond in E. coli peptidoglycan. The enzyme lacks sequence similarity with other peptidases, and is currently classified as a peptidase of unknown fold and catalytic class in all major data bases. Here, we build on our observation that two motifs, characteristic of the newly described LAS group of metallopeptidases, are conserved in MepA-type sequences. We demonstrate that recombinant E. coli MepA is sensitive to metal chelators and that mutations in the predicted Zn2+ ligands His-113, Asp-120, and His-211 inactivate the enzyme. Moreover, we present the crystal structure of MepA. The active site of the enzyme is most similar to the active sites of lysostaphin and D-Ala-D-Ala carboxypeptidase, and the fold is most closely related to the N-domain of sonic hedgehog. We conclude that MepA-type peptidases are LAS enzymes.

Peptidoglycan amidase MepA is a LAS metallopeptidase.,Marcyjaniak M, Odintsov SG, Sabala I, Bochtler M J Biol Chem. 2004 Oct 15;279(42):43982-9. Epub 2004 Jul 29. PMID:15292190<ref>PMID:15292190</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 1tzp" style="background-color:#fffaf0;"></div>

[[Category: Bacillus coli migula 1895]]

[[Category: Bochtler, M]]

[[Category: Marcyjaniak, M]]

[[Category: Odintsov, S G]]

[[Category: Sabala, I]]

[[Category: Peptidoglycan hydrolase]]