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2vbe

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Revision as of 20:54, 12 April 2023

Tailspike protein of bacteriophage Sf6

Structural highlights

2vbe is a 1 chain structure with sequence from Shigella virus Sf6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2vbe"

@@ Line 3: / Line 3: @@
 <StructureSection load='2vbe' size='340' side='right'caption='[[2vbe]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2vbe]] 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=2VBE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VBE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2vbe]] 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=2VBE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VBE FirstGlance]. <br>
-</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
+</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2iym|2iym]], [[2vbk|2vbk]], [[2j3y|2j3y]], [[2iud|2iud]], [[2vbm|2vbm]]</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=2vbe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vbe OCA], [https://pdbe.org/2vbe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vbe RCSB], [https://www.ebi.ac.uk/pdbsum/2vbe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vbe ProSAT]</span></td></tr>
 </table>
 == 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;">
 == Publication Abstract from PubMed ==
@@ Line 27: / Line 25: @@
 __TOC__
 </StructureSection>
-[[Category: Bpsfv]]
 [[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: Oligomeric right-handed parallel beta-helix]]
+[[Category: Seckler R]]
-[[Category: Tailspike]]
-[[Category: Viral adhesion protein]]
-[[Category: Viral protein]]

2vbe

From Proteopedia

Revision as of 20:54, 12 April 2023

Tailspike protein of bacteriophage Sf6

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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