1s8n | pdb_00001s8n
Crystal structure of Rv1626 from Mycobacterium tuberculosis
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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
Page seeded by OCA on Thu Feb 21 14:59:07 2008
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
