1I5C

STRUCTURE OF CHEA DOMAIN P4 IN COMPLEX WITH ADP

1I5C の概要

• エントリーDOI: 10.2210/pdb1i5c/pdb
• 関連するPDBエントリー: 1B3Q
• 分子名称: CHEMOTAXIS PROTEIN CHEA, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: beta-alpha sandwich, signaling protein, transferase
• 由来する生物種: Thermotoga maritima
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 43012.94

構造登録者

Bilwes, A.M.,Quezada, C.M.,Croal, L.R.,Crane, B.R.,Simon, M.I. (登録日: 2001-02-26, 公開日: 2001-08-26, 最終更新日: 2023-08-09)

主引用文献

Bilwes, A.M.,Quezada, C.M.,Croal, L.R.,Crane, B.R.,Simon, M.I.
Nucleotide binding by the histidine kinase CheA.
Nat.Struct.Biol., 8:353-360, 2001

PubMed Abstract: To probe the structural basis for protein histidine kinase (PHK) catalytic activity and the prospects for PHK-specific inhibitor design, we report the crystal structures for the nucleotide binding domain of Thermotoga maritima CheA with ADP and three ATP analogs (ADPNP, ADPCP and TNP-ATP) bound with either Mg(2+) or Mn(2+). The conformation of ADPNP bound to CheA and related ATPases differs from that reported in the ADPNP complex of PHK EnvZ. Interactions of the active site with the nucleotide gamma-phosphate and its associated Mg(2+) ion are linked to conformational changes in an ATP-lid that could mediate recognition of the substrate domain. The inhibitor TNP-ATP binds CheA with its phosphates in a nonproductive conformation and its adenine and trinitrophenyl groups in two adjacent binding pockets. The trinitrophenyl interaction may be exploited for designing CheA-targeted drugs that would not interfere with host ATPases.

PubMed: 11276258
DOI: 10.1038/86243

実験手法

X-RAY DIFFRACTION (1.9 Å)