4jcn
From Proteopedia
(Difference between revisions)
(5 intermediate revisions not shown.) | |||
Line 1: | Line 1: | ||
- | '''Unreleased structure''' | ||
- | + | ==Structure of ESP, serine protease from Staphylococcus epidermidis== | |
+ | <StructureSection load='4jcn' size='340' side='right'caption='[[4jcn]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[4jcn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_epidermidis_ATCC_12228 Staphylococcus epidermidis ATCC 12228]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JCN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JCN 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]] 1.8Å</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=4jcn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jcn OCA], [https://pdbe.org/4jcn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jcn RCSB], [https://www.ebi.ac.uk/pdbsum/4jcn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jcn ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/GSEA_STAES GSEA_STAES] Exhibits a significant hydrolytic activity for the carbonyl side of glutamic acid. Shows activity toward human fibronectin and type 1 collagen (By similarity). | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Staphylococcus epidermidis, a commensal of humans, secretes Esp protease to prevent Staphylococcus aureus biofilm formation and colonization. Blocking S. aureus colonization may reduce the incidence of invasive infectious diseases; however, the mechanism whereby Esp disrupts biofilms is unknown. We show here that Esp cleaves autolysin (Atl)-derived murein hydrolases and prevents staphylococcal release of DNA, which serves as extracellular matrix in biofilms. The three-dimensional structure of Esp was revealed by x-ray crystallography and shown to be highly similar to that of S. aureus V8 (SspA). Both atl and sspA are necessary for biofilm formation, and purified SspA cleaves Atl-derived murein hydrolases. Thus, S. aureus biofilms are formed via the controlled secretion and proteolysis of autolysin, and this developmental program appears to be perturbed by the Esp protease of S. epidermidis. | ||
- | + | Secreted proteases control autolysin-mediated biofilm growth of Staphylococcus aureus.,Chen C, Krishnan V, Macon K, Manne K, Narayana SV, Schneewind O J Biol Chem. 2013 Oct 11;288(41):29440-52. doi: 10.1074/jbc.M113.502039. Epub, 2013 Aug 22. PMID:23970550<ref>PMID:23970550</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
+ | </div> | ||
+ | <div class="pdbe-citations 4jcn" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Staphylococcus epidermidis ATCC 12228]] | ||
+ | [[Category: Krishnan V]] | ||
+ | [[Category: Sthanam VLN]] |
Current revision
Structure of ESP, serine protease from Staphylococcus epidermidis
|