1WCN

NMR structure of the carboxyterminal domains of Escherichia coli NusA

1WCN の概要

• エントリーDOI: 10.2210/pdb1wcn/pdb
• 関連するPDBエントリー: 1U9L 1WCL
• 分子名称: TRANSCRIPTION ELONGATION PROTEIN NUSA (1 entity in total)
• 機能のキーワード: rna-binding protein, escherichia coli nusa, transcription regulation, regulation of rna binding, transcription antitermination and termination, c-terminal repeat units, rna-binding, rna binding protein
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7469.27

構造登録者

Eisenmann, A.,Schwarz, S.,Schweimer, K.,Roesch, P. (登録日: 2004-11-18, 公開日: 2005-08-31, 最終更新日: 2024-05-15)

主引用文献

Eisenmann, A.,Schwarz, S.,Prasch, S.,Schweimer, K.,Roesch, P.
The E. Coli Nusa Carboxy-Terminal Domains are Structurally Similar and Show Specific Rnap- and Lambdan Interactions
Protein Sci., 14:2018-, 2005

PubMed Abstract: The carboxy-terminal domain of the transcription factor Escherichia coli NusA, NusACTD, interacts with the protein N of bacteriophage lambda, lambdaN, and the carboxyl terminus of the E. coli RNA polymerase alpha subunit, alphaCTD. We solved the solution structure of the unbound NusACTD with high-resolution nuclear magnetic resonance (NMR). Additionally, we investigated the binding sites of lambdaN and alphaCTD on NusACTD using NMR titrations. The solution structure of NusACTD shows two structurally similar subdomains, NusA(353-416) and NusA(431-490), matching approximately two homologous acidic sequence repeats. Further characterization of NusACTD with 15N NMR relaxation data suggests that the interdomain region is only weakly structured and that the subdomains are not interacting. Both subdomains adopt an (HhH)2 fold. These folds are normally involved in DNA-protein and protein-protein interactions. NMR titration experiments show clear differences of the interactions of these two domains with alphaCTD and lambdaN, in spite of their structural similarity.

PubMed: 15987884
DOI: 10.1110/PS.051372205

実験手法

SOLUTION NMR