1s8n | pdb_00001s8n
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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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Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- Mycobacterium tuberculosis h37rv
- Single protein
- Feng, V.
- Morth, J.P.
- Perry, L.J.
- Svergun, D.I.
- TBSGC, TB.Structural.Genomics.Consortium.
- Tucker, P.A.
- AZI
- Protein structure initiative
- Psi
- Rv1626
- Structural genomics
- Tb structural genomics consortium
- Tbsgc
- Transcriptional antiterminator
- Two component system
