1j8s: Difference between revisions
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==PAPG ADHESIN RECEPTOR BINDING DOMAIN-UNBOUND FORM== | ==PAPG ADHESIN RECEPTOR BINDING DOMAIN-UNBOUND FORM== | ||
<StructureSection load='1j8s' size='340' side='right' caption='[[1j8s]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1j8s' size='340' side='right' caption='[[1j8s]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1j8s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1j8s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J8S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1J8S FirstGlance]. <br> | ||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1j8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j8s OCA], [http://pdbe.org/1j8s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1j8s RCSB], [http://www.ebi.ac.uk/pdbsum/1j8s PDBsum]</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=1j8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j8s OCA], [http://pdbe.org/1j8s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1j8s RCSB], [http://www.ebi.ac.uk/pdbsum/1j8s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1j8s ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1j8s ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacillus coli migula 1895]] | ||
[[Category: Dodson, K W]] | [[Category: Dodson, K W]] | ||
[[Category: Hultgren, S J]] | [[Category: Hultgren, S J]] | ||
Revision as of 12:45, 4 October 2017
PAPG ADHESIN RECEPTOR BINDING DOMAIN-UNBOUND FORMPAPG ADHESIN RECEPTOR BINDING DOMAIN-UNBOUND FORM
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPapG is the adhesin at the tip of the P pilus that mediates attachment of uropathogenic Escherichia coli to the uroepithelium of the human kidney. The human specific allele of PapG binds to globoside (GbO4), which consists of the tetrasaccharide GalNAc beta 1-3Gal alpha 1-4Gal beta 1-4Glc linked to ceramide. Here, we present the crystal structures of a binary complex of the PapG receptor binding domain bound to GbO4 as well as the unbound form of the adhesin. The biological importance of each of the residues involved in binding was investigated by site-directed mutagenesis. These studies provide a molecular snapshot of a host-pathogen interaction that determines the tropism of uropathogenic E. coli for the human kidney and is critical to the pathogenesis of pyelonephritis. Structural basis of the interaction of the pyelonephritic E. coli adhesin to its human kidney receptor.,Dodson KW, Pinkner JS, Rose T, Magnusson G, Hultgren SJ, Waksman G Cell. 2001 Jun 15;105(6):733-43. PMID:11440716[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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