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| | {{STRUCTURE_1lkt| PDB=1lkt | SCENE= }} | | {{STRUCTURE_1lkt| PDB=1lkt | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF THE HEAD-BINDING DOMAIN OF PHAGE P22 TAILSPIKE PROTEIN'''
| + | ===CRYSTAL STRUCTURE OF THE HEAD-BINDING DOMAIN OF PHAGE P22 TAILSPIKE PROTEIN=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_9135118}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9135118 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9135118}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Telluromethionine]] | | [[Category: Telluromethionine]] |
| | [[Category: Virus protein]] | | [[Category: Virus protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:01:06 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 21:20:37 2008'' |
Revision as of 18:20, 2 July 2008
Template:STRUCTURE 1lkt
CRYSTAL STRUCTURE OF THE HEAD-BINDING DOMAIN OF PHAGE P22 TAILSPIKE PROTEIN
Template:ABSTRACT PUBMED 9135118
About this Structure
1LKT is a Single protein structure of sequence from Enterobacteria phage p22. Full crystallographic information is available from OCA.
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:9135118
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