1tyv: Difference between revisions

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[[Image:1tyv.gif|left|200px]]
{{Seed}}
[[Image:1tyv.png|left|200px]]


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{{STRUCTURE_1tyv|  PDB=1tyv  |  SCENE=  }}  
{{STRUCTURE_1tyv|  PDB=1tyv  |  SCENE=  }}  


'''STRUCTURE OF TAILSPIKE-PROTEIN'''
===STRUCTURE OF TAILSPIKE-PROTEIN===




==Overview==
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The O-antigenic repeating units of lipopolysaccharides from Salmonella serogroups A, B, and D1 serve as receptors for the phage P22 tailspike protein, which also has receptor destroying endoglycosidase (endorhamnosidase) activity, integrating the functions of both hemagglutinin and neuraminidase in influenza virus. Crystal structures of the tailspike protein in complex with oligosaccharides, comprising two O-antigenic repeating units from Salmonella typhimurium, Salmonella enteritidis, and Salmonella typhi 253Ty were determined at 1.8 A resolution. The active-site topology with Asp-392, Asp-395, and Glu-359 as catalytic residues was identified. Kinetics of binding and cleavage suggest a role of the receptor destroying endorhamnosidase activity primarily for detachment of newly assembled phages.
The line below this paragraph, {{ABSTRACT_PUBMED_8855221}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 8855221 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8855221}}


==About this Structure==
==About this Structure==
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[[Category: Recognition]]
[[Category: Recognition]]
[[Category: Viral adhesion protein]]
[[Category: Viral adhesion protein]]
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