1lkt: Difference between revisions
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'''CRYSTAL STRUCTURE OF THE HEAD-BINDING DOMAIN OF PHAGE P22 TAILSPIKE PROTEIN''' | {{Structure | ||
|PDB= 1lkt |SIZE=350|CAPTION= <scene name='initialview01'>1lkt</scene>, resolution 2.6Å | |||
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'''CRYSTAL STRUCTURE OF THE HEAD-BINDING DOMAIN OF PHAGE P22 TAILSPIKE PROTEIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1LKT is a [ | 1LKT is a [[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=1LKT OCA]. | ||
==Reference== | ==Reference== | ||
Phage P22 tailspike protein: crystal structure of the head-binding domain at 2.3 A, fully refined structure of the endorhamnosidase at 1.56 A resolution, and the molecular basis of O-antigen recognition and cleavage., Steinbacher S, Miller S, Baxa U, Budisa N, Weintraub A, Seckler R, Huber R, J Mol Biol. 1997 Apr 11;267(4):865-80. PMID:[http:// | Phage P22 tailspike protein: crystal structure of the head-binding domain at 2.3 A, fully refined structure of the endorhamnosidase at 1.56 A resolution, and the molecular basis of O-antigen recognition and cleavage., Steinbacher S, Miller S, Baxa U, Budisa N, Weintraub A, Seckler R, Huber R, J Mol Biol. 1997 Apr 11;267(4):865-80. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9135118 9135118] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Yersinia phage py54]] | [[Category: Yersinia phage py54]] | ||
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[[Category: virus protein]] | [[Category: virus protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:32:04 2008'' | ||
Revision as of 13:32, 20 March 2008
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CRYSTAL STRUCTURE OF THE HEAD-BINDING DOMAIN OF PHAGE P22 TAILSPIKE PROTEIN
OverviewOverview
The tailspike protein of Salmonella phage P22 is a viral adhesion protein with both receptor binding and destroying activities. It recognises the O-antigenic repeating units of cell surface lipopolysaccharide of serogroup A, B and D1 as receptor, but also inactivates its receptor by endoglycosidase (endorhamnosidase) activity. In the final step of bacteriophage P22 assembly six homotrimeric tailspike molecules are non-covalently attached to the DNA injection apparatus, mediated by their N-terminal, head-binding domains. We report the crystal structure of the head-binding domain of P22 tailspike protein at 2.3 A resolution, solved with a recombinant telluromethionine derivative and non-crystallographic symmetry averaging. The trimeric dome-like structure is formed by two perpendicular beta-sheets of five and three strands, respectively in each subunit and caps a three-helix bundle observed in the structure of the C-terminal receptor binding and cleaving fragment, reported here after full refinement at 1.56 A resolution. In the central part of the receptor binding fragment, three parallel beta-helices of 13 complete turns are associated side-by-side, while the three polypeptide strands merge into a single domain towards their C termini, with close interdigitation at the junction to the beta-helix part. Complex structures with receptor fragments from S. typhimurium, S. enteritidis and S. typhi253Ty determined at 1.8 A resolution are described in detail. Insertions into the beta-helix form the O-antigen binding groove, which also harbours the active site residues Asp392, Asp395 and Glu359. In the intact structure of the tailspike protein, head-binding and receptor-binding parts are probably linked by a flexible hinge whose function may be either to deal with shearing forces on the exposed, 150 A long tailspikes or to allow them to bend during the infection process.
About this StructureAbout this Structure
1LKT is a Single protein structure of sequence from Yersinia phage py54. Full crystallographic information is available from OCA.
ReferenceReference
Phage P22 tailspike protein: crystal structure of the head-binding domain at 2.3 A, fully refined structure of the endorhamnosidase at 1.56 A resolution, and the molecular basis of O-antigen recognition and cleavage., Steinbacher S, Miller S, Baxa U, Budisa N, Weintraub A, Seckler R, Huber R, J Mol Biol. 1997 Apr 11;267(4):865-80. PMID:9135118
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