3CHY

CRYSTAL STRUCTURE OF ESCHERICHIA COLI CHEY REFINED AT 1.7-ANGSTROM RESOLUTION

3CHY の概要

• エントリーDOI: 10.2210/pdb3chy/pdb
• 分子名称: CHEY, SULFATE ION (3 entities in total)
• 機能のキーワード: signal transduction protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14269.33

構造登録者

Volz, K.,Matsumura, P. (登録日: 1991-04-22, 公開日: 1993-01-15, 最終更新日: 2024-02-21)

主引用文献

Volz, K.,Matsumura, P.
Crystal structure of Escherichia coli CheY refined at 1.7-A resolution.
J.Biol.Chem., 266:15511-15519, 1991

PubMed Abstract: The three-dimensional structure of wild-type CheY from Escherichia coli has been refined by stereochemically restrained least squares minimization to a crystallographic R-factor of 15.1% at 1.7-A resolution. The structure contains 1165 atoms, including all atoms of the protein, 147 water molecules, and three sulfate ions. The final model has root mean square deviations of 0.018 and 0.049 A from idealized bond lengths and angle distances, respectively. Seven amino acid side chains have been modeled in dual conformations. CheY folds as a compact (beta/alpha)5 globular protein, with the phosphorylation region contained in a cavity on one face of the molecule. This active site area is bordered by the carboxyl termini of the three central beta-strands, by alpha 1, and by the loop connecting beta 5 to alpha 5. The Lys-109 side chain of this loop extends into the active site by virtue of its cis peptide bond conformation preceding Pro-110. The epsilon-amino group of Lys-109 is in close bonding contact with the carboxyl group of Asp-57, the residue that is phosphorylated in the activation process of CheY. The details of the hydrogen bonding network in the phosphorylation region indicate that structural rearrangements must accompany the phosphorylation of Asp-57.

PubMed: 1869568

実験手法

X-RAY DIFFRACTION (1.66 Å)