1qa1: Difference between revisions

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[[Image:1qa1.png|left|200px]]


{{STRUCTURE_1qa1| PDB=1qa1 | SCENE= }}
==TAILSPIKE PROTEIN, MUTANT V331G==
<StructureSection load='1qa1' size='340' side='right'caption='[[1qa1]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1qa1]] 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=1QA1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QA1 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]] 2&#8491;</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=1qa1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qa1 OCA], [https://pdbe.org/1qa1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qa1 RCSB], [https://www.ebi.ac.uk/pdbsum/1qa1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qa1 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>


===TAILSPIKE PROTEIN, MUTANT V331G===
==See Also==
 
*[[Tailspike protein 3D structures|Tailspike protein 3D structures]]
{{ABSTRACT_PUBMED_10543960}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[1qa1]] is a 1 chain structure with 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=1QA1 OCA].
</StructureSection>
 
[[Category: Large Structures]]
==Reference==
[[Category: Salmonella virus P22]]
<ref group="xtra">PMID:010543960</ref><references group="xtra"/>
[[Category: Baxa U]]
[[Category: Enterobacteria phage p22]]
[[Category: Huber R]]
[[Category: Baxa, U.]]
[[Category: Seckler R]]
[[Category: Huber, R.]]
[[Category: Steinbacher S]]
[[Category: Seckler, R.]]
[[Category: Weintraub A]]
[[Category: Steinbacher, S.]]
[[Category: Weintraub, A.]]
[[Category: Viral protein-receptor complex]]
[[Category: Virus/viral protein]]

Latest revision as of 12:00, 21 February 2024

TAILSPIKE PROTEIN, MUTANT V331GTAILSPIKE PROTEIN, MUTANT V331G

Structural highlights

1qa1 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 2Å
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

1qa1, resolution 2.00Å

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