Crystal structure of an activated response regulator bound to its target.

Published

Journal Article

The 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 beta4-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-beta5-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.

Full Text

Duke Authors

Cited Authors

  • Lee, SY; Cho, HS; Pelton, JG; Yan, D; Henderson, RK; King, DS; Huang, L; Kustu, S; Berry, EA; Wemmer, DE

Published Date

  • January 2001

Published In

Volume / Issue

  • 8 / 1

Start / End Page

  • 52 - 56

PubMed ID

  • 11135671

Pubmed Central ID

  • 11135671

International Standard Serial Number (ISSN)

  • 1072-8368

Digital Object Identifier (DOI)

  • 10.1038/83053

Language

  • eng