1tyv
From Proteopedia
(New page: 200px<br /><applet load="1tyv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tyv, resolution 1.8Å" /> '''STRUCTURE OF TAILSPIK...) |
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| - | [[Image:1tyv.gif|left|200px]]<br /><applet load="1tyv" size=" | + | [[Image:1tyv.gif|left|200px]]<br /><applet load="1tyv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tyv, resolution 1.8Å" /> | caption="1tyv, resolution 1.8Å" /> | ||
'''STRUCTURE OF TAILSPIKE-PROTEIN'''<br /> | '''STRUCTURE OF TAILSPIKE-PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The O-antigenic repeating units of lipopolysaccharides from Salmonella | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1TYV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_phage_py54 Yersinia phage py54]. Full crystallographic information is available from [http:// | + | 1TYV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_phage_py54 Yersinia phage py54]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TYV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: viral adhesion protein]] | [[Category: viral adhesion protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:18:48 2008'' |
Revision as of 13:18, 21 February 2008
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STRUCTURE OF TAILSPIKE-PROTEIN
Overview
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.
About this Structure
1TYV is a Single protein structure of sequence from Yersinia phage py54. Full crystallographic information is available from OCA.
Reference
Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors., Steinbacher S, Baxa U, Miller S, Weintraub A, Seckler R, Huber R, Proc Natl Acad Sci U S A. 1996 Oct 1;93(20):10584-8. PMID:8855221
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