4jpp: Difference between revisions

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{{STRUCTURE_4jpp|  PDB=4jpp  |  SCENE=  }}  
{{STRUCTURE_4jpp|  PDB=4jpp  |  SCENE=  }}  
===Bacteriophage phiX174 H protein residues 143-282===
===Bacteriophage phiX174 H protein residues 143-282===
{{ABSTRACT_PUBMED_24336205}}


==Function==
==Function==
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==Reference==
==Reference==
<references group="xtra"/><references/>
<ref group="xtra">PMID:024336205</ref><references group="xtra"/><references/>
[[Category: Boudko, S B.]]
[[Category: Boudko, S B.]]
[[Category: Fane, B A.]]
[[Category: Fane, B A.]]

Revision as of 07:00, 15 January 2014

Template:STRUCTURE 4jpp

Bacteriophage phiX174 H protein residues 143-282

Template:ABSTRACT PUBMED 24336205

Function

[H_BPPHS] Probably triggers with protein G the injection of the phage DNA into the host upon conformational changes induced by virus-host receptor interaction.[1] [2]

About this Structure

4jpp is a 5 chain structure. Full crystallographic information is available from OCA.

Reference

  1. Sun L, Young LN, Zhang X, Boudko SP, Fokine A, Zbornik E, Roznowski AP, Molineux IJ, Rossmann MG, Fane BA. Icosahedral bacteriophage PhiX174 forms a tail for DNA transport during infection. Nature. 2013 Dec 15. doi: 10.1038/nature12816. PMID:24336205 doi:https://dx.doi.org/10.1038/nature12816
  1. Inagaki M, Tanaka A, Suzuki R, Wakashima H, Kawaura T, Karita S, Nishikawa S, Kashimura N. Characterization of the binding of spike H protein of bacteriophage phiX174 with receptor lipopolysaccharides. J Biochem. 2000 Apr;127(4):577-83. PMID:10739948
  2. Inagaki M, Wakashima H, Kato M, Kaitani K, Nishikawa S. Crucial role of the lipid part of lipopolysaccharide for conformational change of minor spike H protein of bacteriophage phiX174. FEMS Microbiol Lett. 2005 Oct 15;251(2):305-11. PMID:16143459 doi:https://dx.doi.org/10.1016/j.femsle.2005.08.014

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