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1s8n

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Revision as of 21:57, 24 November 2007

Image:1s8n.gif

1s8n, resolution 1.482Å

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Crystal structure of Rv1626 from Mycobacterium tuberculosis

Overview

We describe the crystal structure of Rv1626 from Mycobacterium, tuberculosis at 1.48 A resolution and the corresponding solution structure, determined from small angle X-ray scattering. The N-terminal domain shows, structural homology to the receiver domains found in bacterial, two-component systems. The C-terminal domain has high structural homology, to a recently discovered RNA binding domain involved in transcriptional, antitermination. The molecule in solution was found to be monomeric as it, is in the crystal, but in solution it undergoes a conformational change, that is triggered by changes in ionic strength. This is the first, structure that links the phosphorylation cascade of the two-component, systems with the antitermination event in the transcriptional machinery., Rv1626 belongs to a family of proteins, which we propose calling, phosphorylation-dependent transcriptional antitermination regulators, so, far only found in bacteria, and includes NasT, a protein from the, assimilatory nitrate/nitrite reductase operon of Azetobacter vinelandii.

About this Structure

1S8N is a Single protein structure of sequence from Mycobacterium tuberculosis h37rv with AZI as ligand. Full crystallographic information is available from OCA.

Reference

The crystal and solution structure of a putative transcriptional antiterminator from Mycobacterium tuberculosis., Morth JP, Feng V, Perry LJ, Svergun DI, Tucker PA, Structure. 2004 Sep;12(9):1595-605. PMID:15341725

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