2CHE

STRUCTURE OF THE MG2+-BOUND FORM OF CHEY AND MECHANISM OF PHOSPHORYL TRANSFER IN BACTERIAL CHEMOTAXIS

Summary for 2CHE

• Entry DOI: 10.2210/pdb2che/pdb
• Descriptor: CHEY, MAGNESIUM ION (3 entities in total)
• Functional Keywords: signal transduction protein
• Biological source: Salmonella typhimurium
• Cellular location: Cytoplasm: P0A2D5
• Total number of polymer chains: 1
• Total formula weight: 14033.49

Authors

Stock, A.,Martinez-Hackert, E.,Rasmussen, B.,West, A.,Stock, J.,Ringe, D.,Petsko, G. (deposition date: 1994-01-17, release date: 1994-04-30, Last modification date: 2024-02-14)

Primary citation

Stock, A.M.,Martinez-Hackert, E.,Rasmussen, B.F.,West, A.H.,Stock, J.B.,Ringe, D.,Petsko, G.A.
Structure of the Mg(2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis.
Biochemistry, 32:13375-13380, 1993

PubMed Abstract: The response regulator protein of bacterial chemotaxis, CheY, is representative of a large family of signal transduction proteins that function as phosphorylation-activated switches to regulate the activities of associated effector domains. These regulators catalyze the metal ion-dependent phosphoryl transfer and dephosphorylation reactions that control the effector activities. The crystal structures of Salmonella typhimurium CheY with and without Mg2+ bound at the active site have been determined and refined at 1.8-A resolution. While the overall structures of metal-bound and metal-free CheY are similar, significant rearrangements occur within the active site involving the three most highly conserved residues of the response regulator family. Conservation of the cluster of carboxylate side chains at the active site of response regulator domains can be rationalized in terms of their role in coordinating the catalytically essential divalent metal ion. The Mg2+ coordination geometry provides insights to the mechanism of phosphoryl transfer.

PubMed: 8257674
DOI: 10.1021/bi00212a001

Experimental method

X-RAY DIFFRACTION (1.8 Å)