1ys7
Crystal structure of the response regulator protein prrA complexed with Mg2+Crystal structure of the response regulator protein prrA complexed with Mg2+
Structural highlights
FunctionPRRA_MYCTU Member of the two-component regulatory system PrrB/PrrA. Involved specifically in early intracellular multiplication of Mycobacterium. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. The structural basis of signal transduction for the response regulator PrrA from Mycobacterium tuberculosis.,Nowak E, Panjikar S, Konarev P, Svergun DI, Tucker PA J Biol Chem. 2006 Apr 7;281(14):9659-66. Epub 2006 Jan 23. PMID:16434396[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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