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| | <StructureSection load='2xc1' size='340' side='right'caption='[[2xc1]], [[Resolution|resolution]] 1.65Å' scene=''> | | <StructureSection load='2xc1' size='340' side='right'caption='[[2xc1]], [[Resolution|resolution]] 1.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2xc1]] is a 3 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=2XC1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XC1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2xc1]] is a 3 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=2XC1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XC1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PE4:2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL'>PE4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 1.65Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vfo|2vfo]], [[2vky|2vky]], [[2vfn|2vfn]], [[1tyu|1tyu]], [[1qrc|1qrc]], [[2vfq|2vfq]], [[1clw|1clw]], [[1tyw|1tyw]], [[2vnl|2vnl]], [[1tyx|1tyx]], [[1qrb|1qrb]], [[1tsp|1tsp]], [[1qa2|1qa2]], [[2vfp|2vfp]], [[2vfm|2vfm]], [[1lkt|1lkt]], [[1qa3|1qa3]], [[1qa1|1qa1]], [[1tyv|1tyv]], [[1qq1|1qq1]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PE4:2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL'>PE4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2xc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xc1 OCA], [http://pdbe.org/2xc1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xc1 RCSB], [http://www.ebi.ac.uk/pdbsum/2xc1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xc1 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=2xc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xc1 OCA], [https://pdbe.org/2xc1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xc1 RCSB], [https://www.ebi.ac.uk/pdbsum/2xc1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xc1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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> | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 2xc1" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 2xc1" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Tailspike protein 3D structures|Tailspike protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bpp22]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Heinemann, U]] | + | [[Category: Salmonella virus P22]] |
| - | [[Category: Mueller, J J]] | + | [[Category: Heinemann U]] |
| - | [[Category: Seckler, R]] | + | [[Category: Mueller JJ]] |
| - | [[Category: Seul, A]] | + | [[Category: Seckler R]] |
| - | [[Category: Endoglycosidase]]
| + | [[Category: Seul A]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Salmonella phage p22]]
| + | |
| Structural highlights
Function
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.[1] [2]
Publication Abstract from PubMed
Attachment of phages to host cells, followed by phage DNA ejection, represents the first stage of viral infection of bacteria. Salmonella phage P22 has been extensively studied, serving as an experimental model for bacterial infection by phages. P22 engages bacteria by binding to the sugar moiety of lipopolysaccharides using the viral tailspike protein for attachment. While the structures of the N-terminal particle-binding domain and the major receptor-binding domain of the tailspike have been analyzed individually, the three-dimensional organization of the intact protein, including the highly conserved linker region between the two domains, remained unknown. A single amino-acid exchange in the linker sequence made it possible to crystallize the full-length protein. Two crystal structures of the linker region are presented: one attached to the N-terminal domain and the other present within the complete tailspike protein. Both retain their biological function, but the mutated full-length tailspike displays a retarded folding pathway. Fitting of the full-length tailspike into a published cryo-electron microscopy map of the P22 virion requires an elastic distortion of the crystal structure. The conservation of the linker suggests a role in signal transmission from the distal tip of the molecule to the phage head, eventually leading to DNA ejection.
Bacteriophage P22 tailspike: structure of the complete protein and function of the interdomain linker.,Seul A, Muller JJ, Andres D, Stettner E, Heinemann U, Seckler R Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1336-45. doi:, 10.1107/S1399004714002685. Epub 2014 Apr 30. PMID:24816102[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Weigele PR, Scanlon E, King J. Homotrimeric, beta-stranded viral adhesins and tail proteins. J Bacteriol. 2003 Jul;185(14):4022-30. PMID:12837775
- ↑ Andres D, Hanke C, Baxa U, Seul A, Barbirz S, Seckler R. Tailspike interactions with lipopolysaccharide effect DNA ejection from phage P22 particles in vitro. J Biol Chem. 2010 Nov 19;285(47):36768-75. doi: 10.1074/jbc.M110.169003. Epub, 2010 Sep 3. PMID:20817910 doi:http://dx.doi.org/10.1074/jbc.M110.169003
- ↑ Seul A, Muller JJ, Andres D, Stettner E, Heinemann U, Seckler R. Bacteriophage P22 tailspike: structure of the complete protein and function of the interdomain linker. Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1336-45. doi:, 10.1107/S1399004714002685. Epub 2014 Apr 30. PMID:24816102 doi:http://dx.doi.org/10.1107/S1399004714002685
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