1qa1: Difference between revisions

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 <StructureSection load='1qa1' size='340' side='right'caption='[[1qa1]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1qa1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpp22 Bpp22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QA1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QA1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1qa1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_virus_P22 Salmonella virus P22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QA1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QA1 FirstGlance]. <br>
-</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=1qa1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qa1 OCA], [https://pdbe.org/1qa1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qa1 RCSB], [https://www.ebi.ac.uk/pdbsum/1qa1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qa1 ProSAT]</span></td></tr>
+</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&#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=1qa1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qa1 OCA], [https://pdbe.org/1qa1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qa1 RCSB], [https://www.ebi.ac.uk/pdbsum/1qa1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qa1 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/TSPE_BPP22 TSPE_BPP22]] Non-covalently bound to the neck of the phage capsid and mediating attachment of the viral particle to host cell-surface polysaccharide. It displays endorhamnosidase enzymatic activity, hydrolyzing the alpha-1,3-O-glycosidic linkage between rhamnose and galactose of the O-antigen polysaccharide.<ref>PMID:12837775</ref> <ref>PMID:20817910</ref>
+[https://www.uniprot.org/uniprot/FIBER_BPP22 FIBER_BPP22] Structural component of the short non-contractile tail. The tail comprises six fibers that mediate primary attachment to the host cell lipopolysaccharides (LPS) and display endorhamnosidase enzymatic activity, hydrolyzing the alpha-1,3-O-glycosidic linkage between rhamnose and galactose of the O-antigen polysaccharide. Digestion of the LPS brings the capsid near the cell outer membrane.<ref>PMID:12837775</ref> <ref>PMID:20817910</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
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 __TOC__
 </StructureSection>
-[[Category: Bpp22]]
 [[Category: Large Structures]]
-[[Category: Baxa, U]]
+[[Category: Salmonella virus P22]]
-[[Category: Huber, R]]
+[[Category: Baxa U]]
-[[Category: Seckler, R]]
+[[Category: Huber R]]
-[[Category: Steinbacher, S]]
+[[Category: Seckler R]]
-[[Category: Weintraub, A]]
+[[Category: Steinbacher S]]
-[[Category: Viral protein-receptor complex]]
+[[Category: Weintraub A]]
-[[Category: Virus/viral protein]]