1U8T

Crystal structure of CheY D13K Y106W alone and in complex with a FliM peptide

Summary for 1U8T

• Entry DOI: 10.2210/pdb1u8t/pdb
• Related: 1D4Z 1EHC 1F4V 1FQW 3CHY 5CHY
• Descriptor: Chemotaxis protein cheY, Flagellar motor switch protein fliM, SULFATE ION, ... (4 entities in total)
• Functional Keywords: chey, flim, (beta/alpha)5, signaling protein
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm: P06143; Cell inner membrane; Peripheral membrane protein: P06974
• Total number of polymer chains: 6
• Total formula weight: 60962.56

Authors

Dyer, C.M.,Quillin, M.L.,Campos, A.,Lu, J.,McEvoy, M.M.,Hausrath, A.C.,Westbrook, E.M.,Matsumura, P.,Matthews, B.W.,Dahlquist, F.W. (deposition date: 2004-08-06, release date: 2004-10-05, Last modification date: 2024-10-30)

Primary citation

Dyer, C.M.,Quillin, M.L.,Campos, A.,Lu, J.,McEvoy, M.M.,Hausrath, A.C.,Westbrook, E.M.,Matsumura, P.,Matthews, B.W.,Dahlquist, F.W.
Structure of the Constitutively Active Double Mutant CheY(D13K Y106W) Alone and in Complex with a FliM Peptide
J.Mol.Biol., 342:1325-1335, 2004

PubMed Abstract: CheY is a member of the response regulator protein superfamily that controls the chemotactic swimming response of motile bacteria. The CheY double mutant D13K Y106W (CheY**) is resistant to phosphorylation, yet is a highly effective mimic of phosphorylated CheY in vivo and in vitro. The conformational attributes of this protein that enable it to signal in a phosphorylation-independent manner are unknown. We have solved the crystal structure of selenomethionine-substituted CheY** in the presence of its target, a peptide (FliM16) derived from the flagellar motor switch, FliM, to 1.5A resolution with an R-factor of 19.6%. The asymmetric unit contains four CheY** molecules, two with FliM16 bound, and two without. The two CheY** molecules in the asymmetric unit that are bound to FliM16 adopt a conformation similar to BeF3- -activated wild-type CheY, and also bind FliM16 in a nearly identical manner. The CheY** molecules that do not bind FliM16 are found in a conformation similar to unphosphorylated wild-type CheY, suggesting that the active phenotype of this mutant is enabled by a facile interconversion between the active and inactive conformations. Finally, we propose a ligand-binding model for CheY and CheY**, in which Ile95 changes conformation in a Tyr/Trp106-dependent manner to accommodate FliM.

PubMed: 15351654
DOI: 10.1016/j.jmb.2004.07.084

Experimental method

X-RAY DIFFRACTION (1.5 Å)