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| | ==Crystal structure of the passenger domain of the E. coli autotransporter EspP== | | ==Crystal structure of the passenger domain of the E. coli autotransporter EspP== |
| - | <StructureSection load='3sze' size='340' side='right' caption='[[3sze]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='3sze' size='340' side='right'caption='[[3sze]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3sze]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_0157:h7_edl933 Escherichia coli 0157:h7 edl933]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SZE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SZE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3sze]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_0157:h7_edl933 Escherichia coli 0157:h7 edl933]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SZE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SZE FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ECO57PM78, espP, L7020 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=155864 Escherichia coli 0157:H7 EDL933])</td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ECO57PM78, espP, L7020 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=155864 Escherichia coli 0157:H7 EDL933])</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=3sze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sze OCA], [http://pdbe.org/3sze PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3sze RCSB], [http://www.ebi.ac.uk/pdbsum/3sze PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3sze ProSAT]</span></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=3sze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sze OCA], [https://pdbe.org/3sze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sze RCSB], [https://www.ebi.ac.uk/pdbsum/3sze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sze ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ESPP_ECO57 ESPP_ECO57]] Serine protease capable of cleaving pepsin A and human coagulation factor V, which may contribute to the mucosal hemorrhage observed in hemorrhagic colitis.<ref>PMID:9194704</ref> <ref>PMID:15615856</ref> | + | [[https://www.uniprot.org/uniprot/ESPP_ECO57 ESPP_ECO57]] Serine protease capable of cleaving pepsin A and human coagulation factor V, which may contribute to the mucosal hemorrhage observed in hemorrhagic colitis.<ref>PMID:9194704</ref> <ref>PMID:15615856</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Escherichia coli 0157:h7 edl933]] | | [[Category: Escherichia coli 0157:h7 edl933]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Battaile, K P]] | | [[Category: Battaile, K P]] |
| | [[Category: Chirgadze, N Y]] | | [[Category: Chirgadze, N Y]] |
| Structural highlights
Function
[ESPP_ECO57] Serine protease capable of cleaving pepsin A and human coagulation factor V, which may contribute to the mucosal hemorrhage observed in hemorrhagic colitis.[1] [2]
Publication Abstract from PubMed
Autotransporters represent a large superfamily of known and putative virulence factors produced by Gram-negative bacteria. They consist of an N-terminal "passenger domain" responsible for the specific effector functions of the molecule and a C-terminal "beta-domain" responsible for translocation of the passenger across the bacterial outer membrane. Here, we present the 2.5-A crystal structure of the passenger domain of the extracellular serine protease EspP, produced by the pathogen Escherichia coli O157:H7 and a member of the serine protease autotransporters of Enterobacteriaceae (SPATEs). Like the previously structurally characterized SPATE passenger domains, the EspP passenger domain contains an extended right-handed parallel beta-helix preceded by an N-terminal globular domain housing the catalytic function of the protease. Of note, however, is the absence of a second globular domain protruding from this beta-helix. We describe the structure of the EspP passenger domain in the context of previous results and provide an alternative hypothesis for the function of the beta-helix within SPATEs.
Crystal Structure of the Passenger Domain of the Escherichia coli Autotransporter EspP.,Khan S, Mian HS, Sandercock LE, Chirgadze NY, Pai EF J Mol Biol. 2011 Sep 22. PMID:21964244[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Brunder W, Schmidt H, Karch H. EspP, a novel extracellular serine protease of enterohaemorrhagic Escherichia coli O157:H7 cleaves human coagulation factor V. Mol Microbiol. 1997 May;24(4):767-78. PMID:9194704
- ↑ Szabady RL, Peterson JH, Skillman KM, Bernstein HD. An unusual signal peptide facilitates late steps in the biogenesis of a bacterial autotransporter. Proc Natl Acad Sci U S A. 2005 Jan 4;102(1):221-6. Epub 2004 Dec 22. PMID:15615856 doi:http://dx.doi.org/10.1073/pnas.0406055102
- ↑ Khan S, Mian HS, Sandercock LE, Chirgadze NY, Pai EF. Crystal Structure of the Passenger Domain of the Escherichia coli Autotransporter EspP. J Mol Biol. 2011 Sep 22. PMID:21964244 doi:10.1016/j.jmb.2011.09.028
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