1A63

THE NMR STRUCTURE OF THE RNA BINDING DOMAIN OF E.COLI RHO FACTOR SUGGESTS POSSIBLE RNA-PROTEIN INTERACTIONS, 10 STRUCTURES

1A63 の概要

• エントリーDOI: 10.2210/pdb1a63/pdb
• 分子名称: RHO (1 entity in total)
• 機能のキーワード: transcription termination, termination, rna binding domain, transcription regulation, ob fold
• 由来する生物種: Escherichia coli BL21(DE3)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14634.60

構造登録者

Briercheck, D.M.,Wood, T.C.,Allison, T.J.,Richardson, J.P.,Rule, G.S. (登録日: 1998-03-05, 公開日: 1998-05-27, 最終更新日: 2024-04-10)

主引用文献

Briercheck, D.M.,Wood, T.C.,Allison, T.J.,Richardson, J.P.,Rule, G.S.
The NMR structure of the RNA binding domain of E. coli rho factor suggests possible RNA-protein interactions.
Nat.Struct.Biol., 5:393-399, 1998

PubMed Abstract: Rho protein is an essential hexameric RNA-DNA helicase that binds nascent mRNA transcripts and terminates transcription in a wide variety of eubacterial species. The NMR solution structure of the RNA binding domain of rho, rho130, is presented. This structure consists of two sub-domains, an N-terminal three-helix bundle and a C-terminal beta-barrel that is structurally similar to the oligosaccharide/oligonucleotide binding (OB) fold. Chemical shift changes of rho130 upon RNA binding and previous mutagenetic analyses of intact rho suggest that residues Asp 60, Phe 62, Phe 64, and Arg 66 are critical for binding and support the hypothesis that ssRNA/ssDNA binding is localized in the beta-barrel sub-domain. On the basis of these studies and the tertiary structure of rho130, we propose that residues Asp 60, Phe 62, Phe 64, Arg 66, Tyr 80, Lys 105, and Arg 109 participate in RNA-protein interactions.

PubMed: 9587002
DOI: 10.1038/nsb0598-393

実験手法

SOLUTION NMR