1tyx

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==TITLE OF TAILSPIKE-PROTEIN==
==TITLE OF TAILSPIKE-PROTEIN==
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<StructureSection load='1tyx' size='340' side='right' caption='[[1tyx]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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<StructureSection load='1tyx' size='340' side='right'caption='[[1tyx]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1tyx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpp22 Bpp22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TYX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1tyx]] 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=1TYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TYX FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABE:ABEQUOSE'>ABE</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=RAM:ALPHA-L-RHAMNOSE'>RAM</scene></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]] 1.8&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PHAGE P22 GENE 9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10754 BPP22])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ABE:ABEQUOSE'>ABE</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=RAM:ALPHA-L-RHAMNOSE'>RAM</scene></td></tr>
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<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=1tyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tyx OCA], [http://pdbe.org/1tyx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tyx RCSB], [http://www.ebi.ac.uk/pdbsum/1tyx PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tyx OCA], [https://pdbe.org/1tyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tyx RCSB], [https://www.ebi.ac.uk/pdbsum/1tyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tyx ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The O-antigenic repeating units of lipopolysaccharides from Salmonella serogroups A, B, and D1 serve as receptors for the phage P22 tailspike protein, which also has receptor destroying endoglycosidase (endorhamnosidase) activity, integrating the functions of both hemagglutinin and neuraminidase in influenza virus. Crystal structures of the tailspike protein in complex with oligosaccharides, comprising two O-antigenic repeating units from Salmonella typhimurium, Salmonella enteritidis, and Salmonella typhi 253Ty were determined at 1.8 A resolution. The active-site topology with Asp-392, Asp-395, and Glu-359 as catalytic residues was identified. Kinetics of binding and cleavage suggest a role of the receptor destroying endorhamnosidase activity primarily for detachment of newly assembled phages.
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Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors.,Steinbacher S, Baxa U, Miller S, Weintraub A, Seckler R, Huber R Proc Natl Acad Sci U S A. 1996 Oct 1;93(20):10584-8. PMID:8855221<ref>PMID:8855221</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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==See Also==
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</div>
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*[[Tailspike protein 3D structures|Tailspike protein 3D structures]]
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<div class="pdbe-citations 1tyx" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bpp22]]
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[[Category: Large Structures]]
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[[Category: Huber, R]]
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[[Category: Salmonella virus P22]]
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[[Category: Steinbacher, S]]
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[[Category: Huber R]]
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[[Category: Binding protein lipopolysaccharide]]
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[[Category: Steinbacher S]]
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[[Category: Cell receptor]]
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[[Category: Complex]]
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[[Category: Endoglycosidase carbohydrate]]
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[[Category: Receptor]]
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[[Category: Recognition]]
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[[Category: Viral adhesion protein]]
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Current revision

TITLE OF TAILSPIKE-PROTEIN

PDB ID 1tyx

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