2vfp: Difference between revisions

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[[Image:2vfp.jpg|left|200px]]


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==Low Temperature Structure of P22 Tailspike Protein Fragment (109-666), Mutant V349L==
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<StructureSection load='2vfp' size='340' side='right'caption='[[2vfp]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2vfp]] 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=2VFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VFP FirstGlance]. <br>
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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]] 1.55&#8491;</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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
{{STRUCTURE_2vfp|  PDB=2vfp  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vfp OCA], [https://pdbe.org/2vfp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vfp RCSB], [https://www.ebi.ac.uk/pdbsum/2vfp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vfp ProSAT]</span></td></tr>
</table>
== Function ==
[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>  


===LOW TEMPERATURE STRUCTURE OF P22 TAILSPIKE PROTEIN FRAGMENT (109-666), MUTANT V349L===
==See Also==
 
*[[Tailspike protein 3D structures|Tailspike protein 3D structures]]
 
== References ==
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[[Category: Large Structures]]
{{ABSTRACT_PUBMED_10737931}}
[[Category: Salmonella virus P22]]
 
[[Category: Becker M]]
==About this Structure==
[[Category: Heinemann U]]
2VFP is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p22 Enterobacteria phage p22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VFP OCA].
[[Category: Mueller JJ]]
 
[[Category: Seckler R]]
==Reference==
Plasticity and steric strain in a parallel beta-helix: rational mutations in the P22 tailspike protein., Schuler B, Furst F, Osterroth F, Steinbacher S, Huber R, Seckler R, Proteins. 2000 Apr 1;39(1):89-101. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10737931 10737931]
[[Category: Enterobacteria phage p22]]
[[Category: Becker, M.]]
[[Category: Heinemann, U.]]
[[Category: Mueller, J J.]]
[[Category: Seckler, R.]]
[[Category: Endoglycosidase]]
[[Category: Hydrolase]]
[[Category: Late protein]]
[[Category: P22 tailspike protein]]
[[Category: Protein folding]]
[[Category: Protein stability]]
[[Category: Right-handed parallel beta-helix]]
[[Category: Salmonella bacteriophage p22]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 17 13:15:15 2008''

Latest revision as of 18:18, 13 December 2023

Low Temperature Structure of P22 Tailspike Protein Fragment (109-666), Mutant V349LLow Temperature Structure of P22 Tailspike Protein Fragment (109-666), Mutant V349L

Structural highlights

2vfp is a 1 chain structure with sequence from Salmonella virus P22. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.55Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

See Also

References

  1. Weigele PR, Scanlon E, King J. Homotrimeric, beta-stranded viral adhesins and tail proteins. J Bacteriol. 2003 Jul;185(14):4022-30. PMID:12837775
  2. 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

2vfp, resolution 1.55Å

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