2ID7

1.75 A Structure of T87I Phosphono-CheY

Summary for 2ID7

• Entry DOI: 10.2210/pdb2id7/pdb
• Related: 1C4W
• Descriptor: Chemotaxis protein cheY (2 entities in total)
• Functional Keywords: alpha beta protein flavodoxin-like topology rossman fold, signaling protein
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0AE67
• Total number of polymer chains: 1
• Total formula weight: 14075.25

Authors

Halkides, C.J.,Haas, R.M.,McAdams, K.A.,Casper, E.S.,Santarsiero, B.D.,Mesecar, A.D. (deposition date: 2006-09-14, release date: 2007-09-25, Last modification date: 2023-08-30)

Primary citation

McAdams, K.,Casper, E.S.,Matthew Haas, R.,Santarsiero, B.D.,Eggler, A.L.,Mesecar, A.,Halkides, C.J.
The structures of T87I phosphono-CheY and T87I/Y106W phosphono-CheY help to explain their binding affinities to the FliM and CheZ peptides.
Arch.Biochem.Biophys., 479:105-113, 2008

PubMed Abstract: CheY is a response regulator in bacterial chemotaxis. Escherichia coli CheY mutants T87I and T87I/Y106W CheY are phosphorylatable on Asp57 but unable to generate clockwise rotation of the flagella. To understand this phenotype in terms of structure, stable analogs of the two CheY-P mutants were synthesized: T87I phosphono-CheY and T87I phosphono-CheY. Dissociation constants for peptides derived from flagellar motor protein FliM and phosphatase CheZ were determined for phosphono-CheY and the two mutants. The peptides bind phosphono-CheY almost as strongly as CheY-P; however, they do not bind T87I phosphono-CheY or T87I/Y106W phosphono-CheY, implying that the mutant proteins cannot bind FliM or CheZ tightly in vivo. The structures of T87I phosphono-CheY and T87I/Y106W phosphono-CheY were solved to resolutions of 1.8 and 2.4A, respectively. The increased bulk of I87 forces the side-chain of Y106 or W106, into a more solvent-accessible conformation, which occludes the peptide-binding site.

PubMed: 18801331
DOI: 10.1016/j.abb.2008.08.019

Experimental method

X-RAY DIFFRACTION (1.75 Å)