1EHC

STRUCTURE OF SIGNAL TRANSDUCTION PROTEIN CHEY

1EHC の概要

• エントリーDOI: 10.2210/pdb1ehc/pdb
• 分子名称: CHEY, SULFATE ION (3 entities in total)
• 機能のキーワード: chey, response regulators, chemotaxis, sensory transduction, phosphorylation, flagellar rot, signal transduction
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P06143
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14091.29

構造登録者

Jiang, M.,Bourret, R.,Simon, M.,Volz, K. (登録日: 1996-03-05, 公開日: 1997-05-15, 最終更新日: 2024-02-07)

主引用文献

Jiang, M.,Bourret, R.B.,Simon, M.I.,Volz, K.
Uncoupled phosphorylation and activation in bacterial chemotaxis. The 2.3 A structure of an aspartate to lysine mutant at position 13 of CheY.
J.Biol.Chem., 272:11850-11855, 1997

PubMed Abstract: An aspartate to lysine mutation at position 13 of the chemotaxis regulatory protein CheY causes a constitutive tumbly phenotype when expressed at high copy number in vivo even though the mutant protein is not phosphorylatable. These properties suggest that the D13K mutant adopts the active, signaling conformation of CheY independent of phosphorylation, so knowledge of its structure could explain the activation mechanism of CheY. The x-ray crystallographic structure of the CheY D13K mutant has been solved and refined at 2.3 A resolution to an R-factor of 14.3%. The mutant molecule shows no significant differences in backbone conformation when compared with the wild-type, Mg2+-free structure, but there are localized changes within the active site. The side chain of lysine 13 blocks access to the active site, whereas its epsilon-amino group has no bonding interactions with other groups in the region. Also in the active site, the bond between lysine 109 and aspartate 57 is weakened, and the solvent structure is perturbed. Although the D13K mutant has the inactive conformation in the crystalline form, rearrangements in the active site appear to weaken the overall structure of that region, potentially creating a metastable state of the molecule. If a conformational change is required for signaling by CheY D13K, then it most likely proceeds dynamically, in solution.

PubMed: 9115243
DOI: 10.1074/jbc.272.18.11850

実験手法

X-RAY DIFFRACTION (2.26 Å)