2bnl

From Proteopedia

Revision as of 15:38, 5 November 2007

THE STRUCTURE OF THE N-TERMINAL DOMAIN OF RSBR

Overview

RsbR is a regulator of sigma(B), the RNA polymerase sigma factor subunit, responsible for transcribing the general stress response genes when, environmental stress is imposed on Bacillus subtilis. The C-terminal, domain of RsbR and its paralogues is a substrate for the kinase function, of another sigma(B) regulator, RsbT, but the amino acid sequence of the, N-terminal domain of RsbR does not reveal any obvious biochemical, function. RsbR, its paralogues, and other regulators of sigma(B), including RsbS and RsbT, form large signaling complexes, called, stressosomes. We have determined and present here the crystal structure of, the N-terminal domain of RsbR. Unexpectedly, this structure belongs to the, globin fold superfamily, but there is no bound cofactor. The globin domain, from globin-coupled sensory systems replaces the N-terminal domain of RsbR, in some bacteria, indicating a common genetic ancestry for RsbR and the, globin family. We suggest that the globin fold has been "recycled" in RsbR, and that one more activity can be included in the repertoire of globin, functions, namely the ability to bind signaling macromolecules such as, RsbT.

About this Structure

2BNL is a Single protein structure of sequence from Bacillus subtilis with NA as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.

Reference

Structure of a nonheme globin in environmental stress signaling., Murray JW, Delumeau O, Lewis RJ, Proc Natl Acad Sci U S A. 2005 Nov 29;102(48):17320-5. Epub 2005 Nov 21. PMID:16301540

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