Structural and functional aspects of the sensor histidine kinase PrrB from Mycobacterium tuberculosis

Elzbieta Nowak, Santosh Panjikar, J. Preben Morth, Rositsa Jordanova, Dmitri I. Svergun, Paul A. Tucker

Research output: Contribution to journalArticleResearchpeer-review

33 Citations (Scopus)

Abstract

We describe the solution structures of two- and three-domain constructs of the sensor histidine kinase PrrB from Mycobacterium tuberculosis, which allow us to locate the HAMP linker relative to the ATP binding and dimerization domains. We show that the three-domain construct is active both for autophosphorylation and for phosphotransfer to the cognate response regulator, PrrA. We also describe the high-resolution crystal structure of the catalytic domain alone, and we show that, in solution, it binds ATP. The conformational flexibility of this domain is discussed and related to other structural information.

Original languageEnglish
Pages (from-to)275-285
Number of pages11
JournalStructure
Volume14
Issue number2
DOIs
Publication statusPublished - Feb 2006
Externally publishedYes

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