1qwy

<table><tr><td colspan='2'>[[1qwy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Staa8 Staa8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1QWY FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LytM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=93061 STAA8])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysostaphin Lysostaphin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.75 3.4.24.75] </span></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=1qwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qwy OCA], [http://pdbe.org/1qwy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qwy RCSB], [http://www.ebi.ac.uk/pdbsum/1qwy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qwy ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/LYTM_STAA8 LYTM_STAA8]] Peptidoglycan hydrolase (autolysin) specifically acting on polyglycine interpeptide bridges of the cell wall peptidoglycan.<ref>PMID:10220159</ref> <ref>PMID:8095258</ref>

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== Publication Abstract from PubMed ==

LytM, an autolysin from Staphylococcus aureus, is a Zn(2+)-dependent glycyl-glycine endopeptidase with a characteristic HxH motif that belongs to the lysostaphin-type (MEROPS M23/37) of metallopeptidases. Here, we present the 1.3A crystal structure of LytM, the first structure of a lysostaphin-type peptidase. In the LytM structure, the Zn(2+) is tetrahedrally coordinated by the side-chains of N117, H210, D214 and H293, the second histidine of the HxH motif. Although close to the active-site, H291, the first histidine of the HxH motif, is not directly involved in Zn(2+)-coordination, and there is no water molecule in the coordination sphere of the Zn(2+), suggesting that the crystal structure shows a latent form of the enzyme. Although LytM has not previously been considered as a proenzyme, we show that a truncated version of LytM that lacks the N-terminal part with the poorly conserved Zn(2+) ligand N117 has much higher specific activity than full-length enzyme. This observation is consistent with the known removal of profragments in other lysostaphin-type proteins and with a prior observation of an active LytM degradation fragment in S.aureus supernatant. The "asparagine switch" in LytM is analogous to the "cysteine switch" in pro-matrix metalloproteases.

Latent LytM at 1.3A resolution.,Odintsov SG, Sabala I, Marcyjaniak M, Bochtler M J Mol Biol. 2004 Jan 16;335(3):775-85. PMID:14687573<ref>PMID:14687573</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 1qwy" style="background-color:#fffaf0;"></div>

[[Category: Lysostaphin]]

[[Category: Staa8]]

[[Category: Bochtler, M]]

[[Category: Marcyjaniak, M]]

[[Category: Odintsov, S G]]

[[Category: Sabala, I]]

[[Category: Lytm lysostaphin metalloprotease asparagine switch]]