Nature Structural Biology
8, 52 - 56 (2001)
doi:10.1038/83053
Crystal structure of an activated response regulator bound to its targetSeok-Yong Lee1, 2, Ho S. Cho2, 3, Jeffrey G. Pelton2, Dalai Yan3, Robert K. Henderson2, David S. King4, Li-shar Huang2, Sydney Kustu3, Edward A. Berry2
& David E. Wemmer1, 2, 51
Graduate Group in Biophysics, University of California, Berkeley, California 94720, USA. 2
Physical Biosciences Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, California 94720, USA. 3
Department of Plant and Microbial Biology, University of California, 111 Koshland Hall, Berkeley, California 94720, USA. 4
Howard Hughes Medical Institute and Department of Molecular and Cell Biology, 381 Koshland Hall, University of California, Berkeley, California 94720, USA. 5
Department of Chemistry, University of California, Berkeley, California 94720, USA.
Correspondence should be addressed to David E. Wemmer dewemmer@lbl.govThe chemotactic regulator CheY controls the direction of flagellar rotation in Escherichia coli. We have determined the crystal structure of BeF3
--activated CheY from E. coli in complex with an N-terminal peptide derived from its target, FliM. The structure reveals that the first seven residues of the peptide pack against the  4-H4 loop and helix H4 of CheY in an extended conformation, whereas residues 8−15 form two turns of helix and pack against the H4-5-H5 face. The peptide binds the only region of CheY that undergoes noticeable conformational change upon activation and would most likely be sandwiched between activated CheY and the remainder of FliM to reverse the direction of flagellar rotation.
|
