1LKT

CRYSTAL STRUCTURE OF THE HEAD-BINDING DOMAIN OF PHAGE P22 TAILSPIKE PROTEIN

1LKT の概要

• エントリーDOI: 10.2210/pdb1lkt/pdb
• 分子名称: TAILSPIKE PROTEIN (2 entities in total)
• 機能のキーワード: virus protein, salmonella phage p22, telluromethionine, late protein, viral protein
• 由来する生物種: Enterobacteria phage P22
• 細胞内の位置: Virion (Potential): P12528
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 67846.52

構造登録者

Steinbacher, S. (登録日: 1997-10-17, 公開日: 1998-01-28, 最終更新日: 2024-02-14)

主引用文献

Steinbacher, S.,Miller, S.,Baxa, U.,Budisa, N.,Weintraub, A.,Seckler, R.,Huber, R.
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.
J.Mol.Biol., 267:865-880, 1997

PubMed Abstract: 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.

PubMed: 9135118
DOI: 10.1006/jmbi.1997.0922

実験手法

X-RAY DIFFRACTION (2.6 Å)