The structural basis of signal transduction for the response regulator PrrA from Mycobacterium tuberculosis

Elzbieta Nowak, Santosh Panjikar, Peter Konarev, Dmitri I. Svergun, Paul A. Tucker

Research output: Contribution to journalArticleResearchpeer-review

64 Citations (Scopus)

Abstract

The structure of the two-domain response regulator PrrA from Mycobacterium tuberculosis shows a compact structure in the crystal with a well defined interdomain interface. The interface, which does not include the interdomain linker, makes the recognition helix and the trans-activation loop of the effector domain inaccessible for interaction with DNA. Part of the interface involves hydrogen-bonding interactions of a tyrosine residue in the receiver domain that is believed to be involved in signal transduction, which, if disrupted, would destabilize the interdomain interface, allowing a more extended conformation of the molecule, which would in turn allow access to the recognition helix. In solution, there is evidence for an equilibrium between compact and extended forms of the protein that is far toward the compact form when the protein is inactivated but moves toward a more extended form when activated by the cognate sensor kinase PrrB.

Original languageEnglish
Pages (from-to)9659-9666
Number of pages8
JournalJournal of Biological Chemistry
Volume281
Issue number14
DOIs
Publication statusPublished - 7 Apr 2006
Externally publishedYes

Cite this