1HH2

Crystal structure of NusA from Thermotoga maritima

1HH2 の概要

• エントリーDOI: 10.2210/pdb1hh2/pdb
• 分子名称: N UTILIZATION SUBSTANCE PROTEIN A (2 entities in total)
• 機能のキーワード: transcription regulation, termination
• 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: 37973.29

構造登録者

Worbs, M.,Bourenkov, G.P.,Bartunik, H.D.,Huber, R.,Wahl, M.C. (登録日: 2000-12-18, 公開日: 2001-10-19, 最終更新日: 2024-05-08)

主引用文献

Worbs, M.,Bourenkov, G.P.,Bartunik, H.D.,Huber, R.,Wahl, M.C.
An Extended RNA Binding Surface Through Arrayed S1 and Kh Domains in Transcription Factor Nusa
Mol.Cell, 7:1177-, 2001

PubMed Abstract: The crystal structure of Thermotoga maritima NusA, a transcription factor involved in pausing, termination, and antitermination processes, reveals a four-domain, rod-shaped molecule. An N-terminal alpha/beta portion, a five-stranded beta-barrel (S1 domain), and two K-homology (KH) modules create a continuous spine of positive electrostatic potential, suitable for nonspecific mRNA attraction. Homology models suggest how, in addition, specific mRNA regulatory sequences can be recognized by the S1 and KH motifs. An arrangement of multiple S1 and KH domains mediated by highly conserved residues is seen, creating an extended RNA binding surface, a paradigm for other proteins with similar domain arrays. Structural and mutational analyses indicate that the motifs cooperate, modulating strength and specificity of RNA binding.

PubMed: 11430821
DOI: 10.1016/S1097-2765(01)00262-3

実験手法

X-RAY DIFFRACTION (2.1 Å)