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The solution structure and interactions of CheW from Thermotoga maritima

TitleThe solution structure and interactions of CheW from Thermotoga maritima
Publication TypeJournal Article
Year of Publication2002
AuthorsGriswold, IJ, Zhou, HJ, Matison, M, Swanson, RV, McIntosh, LP, Simon, MI, Dahlquist, FW
JournalNature Structural Biology
Volume9
Pagination121-125
Date PublishedFeb
Type of ArticleArticle
ISBN Number1072-8368
KeywordsBACTERIAL CHEMOTAXIS, BINDING DOMAIN, C-13-LABELED PROTEINS, ESCHERICHIA-COLI, HISTIDINE KINASE, KINASE CHEA, NMR EXPERIMENTS, RESONANCE ASSIGNMENTS, SECONDARY STRUCTURE, SIGNAL-TRANSDUCTION
Abstract

Using protein from the hyperthermophile Thermotoga maritima, we have determined the solution structure of CheW, an essential component in the formation of the bacterial chemotaxis signaling complex. The overall fold is similar to the regulatory domain of the chemotaxis kinase CheA. In addition, interactions of CheW with CheA were monitored by nuclear magnetic resonance (NMR) techniques. The chemical shift perturbation data show the probable contacts that CheW makes with CheA. In combination with previous genetic data, the structure also suggests a possible binding site for the chemotaxis receptor. These results provide a structural basis for a model in which CheW acts as a molecular bridge between CheA and the cytoplasmic tails of the receptor.

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