PDBsum entry 1ffs

Transferase/signaling protein

PDB id: 1ffs

Contents

Protein chains

128 a.a. *

68 a.a. *

Metals

_MN ×2

Waters ×239

* Residue conservation analysis

PDB id:

1ffs

Name:

Transferase/signaling protein

Title:

Chey-binding domain of chea in complex with chey from crystals soaked in acetyl phosphate

Structure:

Chemotaxis protein chey. Chain: a, c. Fragment: residues 124-257. Engineered: yes. Chemotaxis protein chea. Chain: b, d. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Cellular_location: cytoplasm. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PQS)

Resolution:

2.40Å R-factor: 0.217 R-free: 0.255

Authors:

P.Gouet,N.Chinardet,M.Welch,V.Guillet,C.Birck,L.Mourey,J.-P.Samama

Key ref:

P.Gouet et al. (2001). Further insights into the mechanism of function of the response regulator CheY from crystallographic studies of the CheY--CheA(124--257) complex. Acta Crystallogr D Biol Crystallogr, 57, 44-51. PubMed id: 11134926 DOI: 10.1107/S090744490001492X

Date:

26-Jul-00 Release date: 17-Jan-01

Protein chains

P0AE67  (CHEY_ECOLI) -  Chemotaxis protein CheY from Escherichia coli (strain K12)

Seq: 129 a.a.

Struc: 128 a.a.

Protein chains

P07363  (CHEA_ECOLI) -  Chemotaxis protein CheA from Escherichia coli (strain K12)

Seq: 654 a.a.

Struc: 68 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class 2: Chains A, C: E.C.2.7.3.- - ?????
• Enzyme class 3: Chains B, D: E.C.2.7.13.3 - histidine kinase.
• Reaction: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1107/S090744490001492X

Acta Crystallogr D Biol Crystallogr 57:44-51 (2001)

PubMed id: 11134926

Further insights into the mechanism of function of the response regulator CheY from crystallographic studies of the CheY--CheA(124--257) complex.

P.Gouet, N.Chinardet, M.Welch, V.Guillet, S.Cabantous, C.Birck, L.Mourey, J.P.Samama.

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.

Selected figure(s)

Figure 3.
Figure 3 Close-up view at the heterodimer interface illustrating the environment of Tyr106 in CheY and of Glu178, His181 and Phe214 in P2. The 2F[o] - F[c] map of the 2.1 Å resolution native structure is contoured at 1 .

Figure 5.
Figure 5 Stereoview of the bound imido-diphosphate and its network of electrostatic interactions. The 2.7 Å 2F[o] - F[c] map is contoured at 1 .

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2001, 57, 44-51) copyright 2001.

Figures were selected by an automated process.