|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Structure of ESP, serine protease from Staphylococcus epidermidis== | | ==Structure of ESP, serine protease from Staphylococcus epidermidis== |
| - | <StructureSection load='4jcn' size='340' side='right' caption='[[4jcn]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='4jcn' size='340' side='right'caption='[[4jcn]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4jcn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Staes Staes]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JCN FirstGlance]. <br> | + | <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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">esp, gseA, SE_1543 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=176280 STAES])</td></tr> | + | </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> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamyl_endopeptidase Glutamyl endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.19 3.4.21.19] </span></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=4jcn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jcn OCA], [http://pdbe.org/4jcn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4jcn RCSB], [http://www.ebi.ac.uk/pdbsum/4jcn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4jcn ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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). | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 23: |
Line 21: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Glutamyl endopeptidase]] | + | [[Category: Large Structures]] |
| - | [[Category: Staes]] | + | [[Category: Staphylococcus epidermidis ATCC 12228]] |
| - | [[Category: Krishnan, V]] | + | [[Category: Krishnan V]] |
| - | [[Category: Sthanam, V L.N]] | + | [[Category: Sthanam VLN]] |
| - | [[Category: Biofilm]]
| + | |
| - | [[Category: Esp]]
| + | |
| - | [[Category: Extracellular serine protease]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Protease]]
| + | |
| Structural highlights
Function
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).
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chen C, Krishnan V, Macon K, Manne K, Narayana SV, Schneewind O. Secreted proteases control autolysin-mediated biofilm growth of Staphylococcus aureus. J Biol Chem. 2013 Oct 11;288(41):29440-52. doi: 10.1074/jbc.M113.502039. Epub, 2013 Aug 22. PMID:23970550 doi:http://dx.doi.org/10.1074/jbc.M113.502039
|
