2OQR

The structure of the response regulator RegX3 from Mycobacterium tuberculosis

2OQR の概要

• エントリーDOI: 10.2210/pdb2oqr/pdb
• 分子名称: Sensory transduction protein regX3, ACETATE ION, LANTHANUM (III) ION, ... (5 entities in total)
• 機能のキーワード: response regulator, winged-helix-turn-helix, dna-binding, 3d domain swapping, regx3, two component system, transcription, signaling protein
• 由来する生物種: Mycobacterium tuberculosis H37Rv
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25970.39

構造登録者

King-Scott, J. (登録日: 2007-02-01, 公開日: 2007-10-16, 最終更新日: 2023-12-27)

主引用文献

King-Scott, J.,Nowak, E.,Mylonas, E.,Panjikar, S.,Roessle, M.,Svergun, D.I.,Tucker, P.A.
The Structure of a Full-length Response Regulator from Mycobacterium tuberculosis in a Stabilized Three-dimensional Domain-swapped, Activated State.
J.Biol.Chem., 282:37717-37729, 2007

PubMed Abstract: The full-length, two-domain response regulator RegX3 from Mycobacterium tuberculosis is a dimer stabilized by three-dimensional domain swapping. Dimerization is known to occur in the OmpR/PhoB subfamily of response regulators upon activation but has previously only been structurally characterized for isolated receiver domains. The RegX3 dimer has a bipartite intermolecular interface, which buries 2357 A(2) per monomer. The two parts of the interface are between the two receiver domains (dimerization interface) and between a composite receiver domain and the effector domain of the second molecule (interdomain interface). The structure provides support for the importance of threonine and tyrosine residues in the signal transduction mechanism. These residues occur in an active-like conformation stabilized by lanthanum ions. In solution, RegX3 exists as both a monomer and a dimer in a concentration-dependent equilibrium. The dimer in solution differs from the active form observed in the crystal, resembling instead the model of the inactive full-length response regulator PhoB.

PubMed: 17942407
DOI: 10.1074/jbc.M705081200

実験手法

X-RAY DIFFRACTION (2.03 Å)