1FFG

CHEY-BINDING DOMAIN OF CHEA IN COMPLEX WITH CHEY AT 2.1 A RESOLUTION

1FFG の概要

• エントリーDOI: 10.2210/pdb1ffg/pdb
• 関連するPDBエントリー: 1A0O 1FFS 1FFW
• 分子名称: CHEMOTAXIS PROTEIN CHEY, CHEMOTAXIS PROTEIN CHEA, MANGANESE (II) ION, ... (4 entities in total)
• 機能のキーワード: doubly wound (beta/alpha)5 fold, transferase-signaling protein complex, transferase/signaling protein
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cytoplasm: P07363
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 57082.90

構造登録者

Gouet, P.,Chinardet, N.,Welch, M.,Guillet, V.,Birck, C.,Mourey, L.,Samama, J.-P. (登録日: 2000-07-25, 公開日: 2001-01-17, 最終更新日: 2024-02-07)

主引用文献

Gouet, P.,Chinardet, N.,Welch, M.,Guillet, V.,Cabantous, S.,Birck, C.,Mourey, L.,Samama, J.P.
Further insights into the mechanism of function of the response regulator CheY from crystallographic studies of the CheY--CheA(124--257) complex.
Acta Crystallogr.,Sect.D, 57:44-51, 2001

PubMed Abstract: New crystallographic structures of the response regulator CheY in association with CheA(124--257), its binding domain in the kinase CheA, have been determined. In all crystal forms, the molecular interactions at the heterodimer interface are identical. Soaking experiments have been performed on the crystals using acetyl phosphate as phosphodonor to CheY. No phosphoryl group attached to Asp57 of CheY is visible from the electron density, but the response regulator in the CheY-CheA(124--257) complex may have undergone a phosphorylation-dephosphorylation process. The distribution of water molecules and the geometry of the active site have changed and are now similar to those of isolated CheY. In a second soaking experiment, imido-diphosphate, an inhibitor of the phosphorylation reaction, was used. This compound binds in the vicinity of the active site, close to the N-terminal part of the first alpha-helix. Together, these results suggest that the binding of CheY to CheA(124--257) generates a geometry of the active site that favours phosphorylation and that imido-diphosphate interferes with phosphorylation by precluding structural changes in this region.

PubMed: 11134926
DOI: 10.1107/S090744490001492X

実験手法

X-RAY DIFFRACTION (2.1 Å)