1SD5

Crystal structure of Rv1626

Summary for 1SD5

• Entry DOI: 10.2210/pdb1sd5/pdb
• Related: 1S8N
• Descriptor: putative antiterminator, IODIDE ION (3 entities in total)
• Functional Keywords: rv1626, transcriptional, antiterminator, two components system, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, unknown function
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 24603.72

Authors

Morth, J.P.,Feng, V.,Perry, L.J.,Svergun, D.I.,Tucker, P.A.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2004-02-13, release date: 2004-09-21, Last modification date: 2024-02-14)

Primary citation

Morth, J.P.,Feng, V.,Perry, L.J.,Svergun, D.I.,Tucker, P.A.
The Crystal and Solution Structure of a Putative Transcriptional Antiterminator from Mycobacterium tuberculosis.
Structure, 12:1595-1605, 2004

PubMed Abstract: 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.

PubMed: 15341725
DOI: 10.1016/j.str.2004.06.018

Experimental method

X-RAY DIFFRACTION (1.68 Å)