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< | ==Low Temperature Structure of P22 Tailspike Protein Fragment (109-666), Mutant V349L== | ||
<StructureSection load='2vfp' size='340' side='right'caption='[[2vfp]], [[Resolution|resolution]] 1.55Å' scene=''> | |||
== Structural highlights == | |||
<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> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55Å</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=SO4:SULFATE+ION'>SO4</scene></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=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> | |||
=== | ==See Also== | ||
*[[Tailspike protein 3D structures|Tailspike protein 3D structures]] | |||
== References == | |||
< | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Salmonella virus P22]] | |||
[[Category: Becker M]] | |||
[[Category: Heinemann U]] | |||
[[Category: Mueller JJ]] | |||
[[Category: Seckler R]] | |||
[[Category: | |||
[[Category: Becker | |||
[[Category: Heinemann | |||
[[Category: Mueller | |||
[[Category: Seckler | |||
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
FunctionFIBER_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 AlsoReferences
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