2fmk Citations

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 359 624-45 (2006)
Related entries: 2fka, 2flk, 2flw, 2fmf, 2fmh, 2fmi

Cited: 36 times
EuropePMC logo PMID: 16674976

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.

Articles - 2fmk mentioned but not cited (4)

  1. 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. Guhaniyogi J, Robinson VL, Stock AM. J Mol Biol 359 624-645 (2006)
  2. Interaction of CheY with the C-terminal peptide of CheZ. Guhaniyogi J, Wu T, Patel SS, Stock AM. J Bacteriol 190 1419-1428 (2008)
  3. Protein-protein interaction network prediction by using rigid-body docking tools: application to bacterial chemotaxis. Matsuzaki Y, Ohue M, Uchikoga N, Akiyama Y. Protein Pept Lett 21 790-798 (2014)
  4. Structural characterization of the ANTAR antiterminator domain bound to RNA. Walshe JL, Siddiquee R, Patel K, Ataide SF. Nucleic Acids Res 50 2889-2904 (2022)


Reviews citing this publication (2)

  1. Bacterial response regulators: versatile regulatory strategies from common domains. Gao R, Mack TR, Stock AM. Trends Biochem Sci 32 225-234 (2007)
  2. Auxiliary phosphatases in two-component signal transduction. Silversmith RE. Curr Opin Microbiol 13 177-183 (2010)

Articles citing this publication (30)