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NMR structure of activated CheY.

Abstract：

: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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

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

doi

10.1006/jmbi.2000.3595

keywords:

subject

Has Abstract

pub_date

2000-03-31 00:00:00

pages

543-51

issue

3

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(00)93595-2

journal_volume

297

pub_type

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