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| | <StructureSection load='2vbm' size='340' side='right'caption='[[2vbm]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='2vbm' size='340' side='right'caption='[[2vbm]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2vbm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpsfv Bpsfv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VBM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VBM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2vbm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Shigella_virus_Sf6 Shigella virus Sf6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VBM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VBM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=RAM:ALPHA-L-RHAMNOSE'>RAM</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=RAM:ALPHA-L-RHAMNOSE'>RAM</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2vbe|2vbe]], [[2vbk|2vbk]]</div></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=2vbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vbm OCA], [https://pdbe.org/2vbm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vbm RCSB], [https://www.ebi.ac.uk/pdbsum/2vbm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vbm 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=2vbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vbm OCA], [https://pdbe.org/2vbm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vbm RCSB], [https://www.ebi.ac.uk/pdbsum/2vbm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vbm ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/TSPE_BPSFV TSPE_BPSFV]] 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.
| + | [https://www.uniprot.org/uniprot/FIBER_BPSFV FIBER_BPSFV] 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:18462681</ref> <ref>PMID:12424253</ref> <ref>PMID:6284</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bpsfv]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Barbirz, S]] | + | [[Category: Shigella virus Sf6]] |
| - | [[Category: Freiberg, A]] | + | [[Category: Barbirz S]] |
| - | [[Category: Heinemann, U]] | + | [[Category: Freiberg A]] |
| - | [[Category: Mueller, J J]] | + | [[Category: Heinemann U]] |
| - | [[Category: Seckler, R]] | + | [[Category: Mueller JJ]] |
| - | [[Category: Endorhamnosidase]]
| + | [[Category: Seckler R]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Right-handed parallel beta-helix]]
| + | |
| - | [[Category: Tailspike]]
| + | |
| - | [[Category: Viral adhesion protein]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
FIBER_BPSFV 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.[1] [2] [3]
Publication Abstract from PubMed
Sf6 belongs to the Podoviridae family of temperate bacteriophages that infect gram-negative bacteria by insertion of their double-stranded DNA. They attach to their hosts specifically via their tailspike proteins. The 1.25 A crystal structure of Shigella phage Sf6 tailspike protein (Sf6 TSP) reveals a conserved architecture with a central, right-handed beta helix. In the trimer of Sf6 TSP, the parallel beta helices form a left-handed, coiled-beta coil with a pitch of 340 A. The C-terminal domain consists of a beta sandwich reminiscent of viral capsid proteins. Further crystallographic and biochemical analyses show a Shigella cell wall O-antigen fragment to bind to an endorhamnosidase active site located between two beta-helix subunits each anchoring one catalytic carboxylate. The functionally and structurally related bacteriophage, P22 TSP, lacks sequence identity with Sf6 TSP and has its active sites on single subunits. Sf6 TSP may serve as an example for the evolution of different host specificities on a similar general architecture.
An intersubunit active site between supercoiled parallel beta helices in the trimeric tailspike endorhamnosidase of Shigella flexneri Phage Sf6.,Muller JJ, Barbirz S, Heinle K, Freiberg A, Seckler R, Heinemann U Structure. 2008 May;16(5):766-75. PMID:18462681[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Muller JJ, Barbirz S, Heinle K, Freiberg A, Seckler R, Heinemann U. An intersubunit active site between supercoiled parallel beta helices in the trimeric tailspike endorhamnosidase of Shigella flexneri Phage Sf6. Structure. 2008 May;16(5):766-75. PMID:18462681 doi:10.1016/j.str.2008.01.019
- ↑ Freiberg A, Morona R, Van den Bosch L, Jung C, Behlke J, Carlin N, Seckler R, Baxa U. The tailspike protein of Shigella phage Sf6. A structural homolog of Salmonella phage P22 tailspike protein without sequence similarity in the beta-helix domain. J Biol Chem. 2003 Jan 17;278(3):1542-8. PMID:12424253 doi:10.1074/jbc.M205294200
- ↑ Iwashita S, Kanegasaki S. Enzymic and molecular properties of base-plate parts of bacteriophage P22. Eur J Biochem. 1976 May 17;65(1):87-94. PMID:6284 doi:10.1111/j.1432-1033.1976.tb10392.x
- ↑ Muller JJ, Barbirz S, Heinle K, Freiberg A, Seckler R, Heinemann U. An intersubunit active site between supercoiled parallel beta helices in the trimeric tailspike endorhamnosidase of Shigella flexneri Phage Sf6. Structure. 2008 May;16(5):766-75. PMID:18462681 doi:10.1016/j.str.2008.01.019
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