PDBsum entry: 1c4w

Signaling protein

PDB id: 1c4w

Contents

Protein chain

128 a.a. *

Waters ×140

* Residue conservation analysis

PDB id:

1c4w

Name:

Signaling protein

Title:

1.9 a structure of a-thiophosphonate modified chey d57c

Structure:

Chemotaxis protein chey. Chain: a. Engineered: yes. Mutation: yes

Source:

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

Resolution:

1.84Å R-factor: 0.208

Authors:

C.J.Halkides,M.M.Mcevoy,P.Matsumura,K.Volz,F.W.Dahlquist

Key ref:

C.J.Halkides et al. (2000). The 1.9 A resolution crystal structure of phosphono-CheY, an analogue of the active form of the response regulator, CheY. Biochemistry, 39, 5280-5286. PubMed id: 10819997 DOI: 10.1021/bi9925524

Date:

28-Sep-99 Release date: 08-May-00

Protein chain

P0AE67  (CHEY_ECOLI) -  Chemotaxis protein CheY

Seq: 129 a.a.

Struc: 128 a.a.*

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

 Gene Ontology (GO) functional annotation 

• Cellular component: cytoplasm (1 term)
• Biological process: intracellular signal transduction (7 terms)
• Biochemical function: two-component response regulator activity (3 terms)

DOI no: 10.1021/bi9925524

Biochemistry 39:5280-5286 (2000)

PubMed id: 10819997

The 1.9 A resolution crystal structure of phosphono-CheY, an analogue of the active form of the response regulator, CheY.

C.J.Halkides, M.M.McEvoy, E.Casper, P.Matsumura, K.Volz, F.W.Dahlquist.

ABSTRACT

To structurally characterize the activated state of the transiently phosphorylated signal transduction protein CheY, we have constructed an alpha-thiophosphonate derivative of the CheY D57C point mutant and determined its three-dimensional structure at 1.85 A resolution. We have also characterized this analogue with high-resolution NMR and studied its binding to a peptide derived from FliM, CheY's target component of the flagellar motor. The chemically modified derivative, phosphono-CheY, exhibits many of the chemical properties of phosphorylated wild-type CheY, except that it is indefinitely stable. Electron density for the alpha-thiophosphonate substitution is clear and readily interpretable; omit refinement density at the phosphorus atom is greater than 10sigma. The molecule shows a number of localized conformational changes that are believed to constitute the postphosphorylation activation events. The most obvious of these changes include movement of the side chain of the active site base, Lys 109, and a predominately buried conformation of the side chain of Tyr 106. In addition, there are a number of more subtle changes more distant from the active site involving the alpha4 and alpha5 helices. These results are consistent with our previous structural interpretations of other CheY activation mutants, and with our earlier hypotheses concerning CheY activation through propagation of structural changes away from the active site.