1sd5

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spinqualitylabelsall models 1sd5, resolution 1.68Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of Rv1626

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

1SD5 is a Single protein structure of sequence from Mycobacterium tuberculosis h37rv with IOD 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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