1SD5

Crystal structure of Rv1626

1SD5 の概要

• エントリーDOI: 10.2210/pdb1sd5/pdb
• 関連するPDBエントリー: 1S8N
• 分子名称: putative antiterminator, IODIDE ION (3 entities in total)
• 機能のキーワード: rv1626, transcriptional, antiterminator, two components system, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, unknown function
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24603.72

構造登録者

Morth, J.P.,Feng, V.,Perry, L.J.,Svergun, D.I.,Tucker, P.A.,TB Structural Genomics Consortium (TBSGC) (登録日: 2004-02-13, 公開日: 2004-09-21, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.68 Å)