1FFG

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

Summary for 1FFG

• Entry DOI: 10.2210/pdb1ffg/pdb
• Related: 1A0O 1FFS 1FFW
• Descriptor: CHEMOTAXIS PROTEIN CHEY, CHEMOTAXIS PROTEIN CHEA, MANGANESE (II) ION, ... (4 entities in total)
• Functional Keywords: doubly wound (beta/alpha)5 fold, transferase-signaling protein complex, transferase/signaling protein
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm: P07363
• Total number of polymer chains: 4
• Total formula weight: 57082.90

Authors

Gouet, P.,Chinardet, N.,Welch, M.,Guillet, V.,Birck, C.,Mourey, L.,Samama, J.-P. (deposition date: 2000-07-25, release date: 2001-01-17, Last modification date: 2024-02-07)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.1 Å)