1lkt: Difference between revisions

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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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-[[Image:1lkt.jpg|left|200px]]<br /><applet load="1lkt" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1lkt, resolution 2.6&Aring;" />
 '''CRYSTAL STRUCTURE OF THE HEAD-BINDING DOMAIN OF PHAGE P22 TAILSPIKE PROTEIN'''<br />
 ==Overview==
-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 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 Structure==
-LKT 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LKT OCA].
+LKT 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=1LKT OCA].
 ==Reference==
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 [[Category: virus protein]]
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