1KGS

Crystal Structure at 1.50 A of an OmpR/PhoB Homolog from Thermotoga maritima

1KGS の概要

• エントリーDOI: 10.2210/pdb1kgs/pdb
• 分子名称: DNA BINDING RESPONSE REGULATOR D, THIOCYANATE ION (3 entities in total)
• 機能のキーワード: dna-binding protein, alph-beta sandwich, winged-helix, helix-turn-helix, response regulator, dna binding protein
• 由来する生物種: Thermotoga maritima
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26826.85

構造登録者

Buckler, D.R.,Zhou, Y.,Stock, A.M. (登録日: 2001-11-28, 公開日: 2001-12-05, 最終更新日: 2024-10-16)

主引用文献

Buckler, D.R.,Zhou, Y.,Stock, A.M.
Evidence of intradomain and interdomain flexibility in an OmpR/PhoB homolog from Thermotoga maritima.
Structure, 10:153-164, 2002

PubMed Abstract: Two-component systems, the predominant signal transduction strategy used by prokaryotes, involve phosphorelay from a sensor histidine kinase (HK) to an intracellular response regulator protein (RR) that typically acts as a transcription regulator. RRs are modular proteins, usually composed of a conserved regulatory domain, which functions as a phosphorylation-activated switch, and an attached DNA binding effector domain. The crystal structure of a Thermotoga maritima transcription factor, DrrD, has been determined at 1.5 A resolution, providing the first structural information for a full-length member of the OmpR/PhoB subfamily of RRs. A small interdomain interface occurs between alpha 5 of the regulatory domain and an antiparallel sheet of the effector domain. The lack of an extensive interface in the unphosphorylated protein distinguishes DrrD from other structurally characterized multidomain RRs and suggests a different mode of interdomain regulation.

PubMed: 11839301
DOI: 10.1016/S0969-2126(01)00706-7

実験手法

X-RAY DIFFRACTION (1.5 Å)