1w53

From Proteopedia

Revision as of 08:19, 3 February 2008

KINASE RECRUITMENT DOMAIN OF THE STRESS PHOSPHATASE RSBU

Overview

RsbU is a positive regulator of the activity of sigmaB, the general, stress-response sigma factor of Gram+ microorganisms. The N-terminal, domain of this protein has no significant sequence homology with proteins, of known function, whereas the C-terminal domain is similar to the, catalytic domains of PP2C-type phosphatases. The phosphatase activity of, RsbU is stimulated greatly during the response to stress by associating, with a kinase, RsbT. This association leads to the induction of sigmaB, activity. Here we present data on the activation process and demonstrate, in vivo that truncations in the N-terminal region of RsbU are deleterious, for the activation of RsbU. This conclusion is supported by comparisons of, the phosphatase activities of full-length and a truncated form of RsbU in, vitro. Our determination of the crystal structure of the N-terminal domain, of RsbU from Bacillus subtilis reveals structural similarities to the, regulatory domains from ubiquitous protein phosphatases and a conserved, domain of sigma-factors, illuminating the activation processes of, phosphatases and the evolution of "partner switching." Finally, the, molecular basis of kinase recruitment by the RsbU phosphatase is discussed, by comparing RsbU sequences from bacteria that either possess or lack, RsbT.

About this Structure

1W53 is a Single protein structure of sequence from Bacillus subtilis with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Functional and structural characterization of RsbU, a stress signaling protein phosphatase 2C., Delumeau O, Dutta S, Brigulla M, Kuhnke G, Hardwick SW, Volker U, Yudkin MD, Lewis RJ, J Biol Chem. 2004 Sep 24;279(39):40927-37. Epub 2004 Jul 19. PMID:15263010

Page seeded by OCA on Sun Feb 3 10:19:25 2008