NMR structure of activated CheY.

Journal Article (Journal Article)

The CheY protein is the response regulator in bacterial chemotaxis. Phosphorylation of a conserved aspartyl residue induces structural changes that convert the protein from an inactive to an active state. The short half-life of the aspartyl-phosphate has precluded detailed structural analysis of the active protein. Persistent activation of Escherichia coli CheY was achieved by complexation with beryllofluoride (BeF(3)(-)) and the structure determined by NMR spectroscopy to a backbone r.m.s.d. of 0.58(+/-0.08) A. Formation of a hydrogen bond between the Thr87 OH group and an active site acceptor, presumably Asp57.BeF(3)(-), stabilizes a coupled rearrangement of highly conserved residues, Thr87 and Tyr106, along with displacement of beta4 and H4, to yield the active state. The coupled rearrangement may be a more general mechanism for activation of receiver domains.

Full Text

Duke Authors

Cited Authors

  • Cho, HS; Lee, SY; Yan, D; Pan, X; Parkinson, JS; Kustu, S; Wemmer, DE; Pelton, JG

Published Date

  • March 31, 2000

Published In

Volume / Issue

  • 297 / 3

Start / End Page

  • 543 - 551

PubMed ID

  • 10731410

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1006/jmbi.2000.3595


  • eng

Conference Location

  • Netherlands