Structural highlights
FunctionPDTAR_MYCTU Member of the two-component regulatory system pdtaR/pdtaS.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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