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3sze
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| - | [[ | + | ==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=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3sze]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_o157:h7 Escherichia coli o157:h7]. 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> | ||
| + | </td></tr><tr><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=83334 Escherichia coli O157:H7])</td></tr> | ||
| + | <tr><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://www.rcsb.org/pdb/explore.do?structureId=3sze RCSB], [http://www.ebi.ac.uk/pdbsum/3sze PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:21964244</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | < | + | <references/> |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
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[[Category: Escherichia coli o157:h7]] | [[Category: Escherichia coli o157:h7]] | ||
[[Category: Battaile, K P.]] | [[Category: Battaile, K P.]] | ||
Revision as of 05:29, 5 June 2014
Crystal structure of the passenger domain of the E. coli autotransporter EspP
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