1kmi

Structural highlights

Function

[CHEY_ECOLI] Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. In its active (phosphorylated or acetylated) form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor which induces a change from counterclockwise to clockwise flagellar rotation. Overexpression of CheY in association with MotA and MotB improves motility of a ycgR disruption, suggesting there is an interaction (direct or indirect) between the c-di-GMP-binding flagellar brake protein and the flagellar stator.^[1] [CHEZ_ECOLI] Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P).^{[2] [3]}

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

• Chemotaxis protein

References

1. ↑ Paul K, Nieto V, Carlquist WC, Blair DF, Harshey RM. The c-di-GMP binding protein YcgR controls flagellar motor direction and speed to affect chemotaxis by a "backstop brake" mechanism. Mol Cell. 2010 Apr 9;38(1):128-39. doi: 10.1016/j.molcel.2010.03.001. Epub 2010, Mar 25. PMID:20346719 doi:10.1016/j.molcel.2010.03.001
2. ↑ Wang H, Matsumura P. Characterization of the CheAS/CheZ complex: a specific interaction resulting in enhanced dephosphorylating activity on CheY-phosphate. Mol Microbiol. 1996 Feb;19(4):695-703. PMID:8820640
3. ↑ Boesch KC, Silversmith RE, Bourret RB. Isolation and characterization of nonchemotactic CheZ mutants of Escherichia coli. J Bacteriol. 2000 Jun;182(12):3544-52. PMID:10852888
4. ↑ Zhao R, Collins EJ, Bourret RB, Silversmith RE. Structure and catalytic mechanism of the E. coli chemotaxis phosphatase CheZ. Nat Struct Biol. 2002 Aug;9(8):570-5. PMID:12080332 doi:10.1038/nsb816