3sze

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Current revision (09:58, 1 March 2024) (edit) (undo)
 
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<StructureSection load='3sze' size='340' side='right'caption='[[3sze]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='3sze' size='340' side='right'caption='[[3sze]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<table><tr><td colspan='2'>[[3sze]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7_str._EDL933 Escherichia coli O157:H7 str. 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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</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>
<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 ==
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[[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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:21964244</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3sze" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Escherichia coli 0157:h7 edl933]]
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[[Category: Escherichia coli O157:H7 str. EDL933]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Battaile, K P]]
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[[Category: Battaile KP]]
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[[Category: Chirgadze, N Y]]
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[[Category: Chirgadze NY]]
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[[Category: Khan, S]]
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[[Category: Khan S]]
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[[Category: Lam, R]]
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[[Category: Lam R]]
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[[Category: Mian, H S]]
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[[Category: Mian HS]]
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[[Category: Pai, E F]]
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[[Category: Pai EF]]
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[[Category: Sandercock, L E]]
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[[Category: Sandercock LE]]
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[[Category: Hydrolase]]
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[[Category: Parallel beta-helix]]
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[[Category: Serine protease]]
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Current revision

Crystal structure of the passenger domain of the E. coli autotransporter EspP

PDB ID 3sze

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