2FMK

Crystal structure of Mg2+ and BeF3- bound CheY in complex with CheZ 200-214 solved from a P2(1)2(1)2 crystal grown in MES (pH 6.0)

Summary for 2FMK

• Entry DOI: 10.2210/pdb2fmk/pdb
• Related: 2FKA 2FLK 2FLW 2FMF 2FMH 2FMI
• Descriptor: Chemotaxis protein cheY, C-terminal 15-mer from Chemotaxis protein cheZ, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: chemotaxis; bef(3)(-)-bound chey; chey-chez peptide complex, signaling protein
• Biological source: Salmonella typhimurium; More
• Cellular location: Cytoplasm: P0A2D5 P07800
• Total number of polymer chains: 2
• Total formula weight: 15879.42

Authors

Guhaniyogi, J.,Robinson, V.L.,Stock, A.M. (deposition date: 2006-01-09, release date: 2006-05-23, Last modification date: 2024-10-30)

Primary citation

Guhaniyogi, J.,Robinson, V.L.,Stock, A.M.
Crystal Structures of Beryllium Fluoride-free and Beryllium Fluoride-bound CheY in Complex with the Conserved C-terminal Peptide of CheZ Reveal Dual Binding Modes Specific to CheY Conformation
J.Mol.Biol., 359:624-645, 2006

PubMed Abstract: Chemotaxis, the environment-specific swimming behavior of a bacterial cell is controlled by flagellar rotation. The steady-state level of the phosphorylated or activated form of the response regulator CheY dictates the direction of flagellar rotation. CheY phosphorylation is regulated by a fine equilibrium of three phosphotransfer activities: phosphorylation by the kinase CheA, its auto-dephosphorylation and dephosphorylation by its phosphatase CheZ. Efficient dephosphorylation of CheY by CheZ requires two spatially distinct protein-protein contacts: tethering of the two proteins to each other and formation of an active site for dephosphorylation. The former involves interaction of phosphorylated CheY with the small highly conserved C-terminal helix of CheZ (CheZ(C)), an indispensable structural component of the functional CheZ protein. To understand how the CheZ(C) helix, representing less than 10% of the full-length protein, ascertains molecular specificity of binding to CheY, we have determined crystal structures of CheY in complex with a synthetic peptide corresponding to 15 C-terminal residues of CheZ (CheZ(200-214)) at resolutions ranging from 2.0 A to 2.3A. These structures provide a detailed view of the CheZ(C) peptide interaction both in the presence and absence of the phosphoryl analog, BeF3-. Our studies reveal that two different modes of binding the CheZ(200-214) peptide are dictated by the conformational state of CheY in the complex. Our structures suggest that the CheZ(C) helix binds to a "meta-active" conformation of inactive CheY and it does so in an orientation that is distinct from the one in which it binds activated CheY. Our dual binding mode hypothesis provides implications for reverse information flow in CheY and extends previous observations on inherent resilience in CheY-like signaling domains.

PubMed: 16674976
DOI: 10.1016/j.jmb.2006.03.050

Experimental method

X-RAY DIFFRACTION (1.999 Å)