1WCN

NMR structure of the carboxyterminal domains of Escherichia coli NusA

Summary for 1WCN

• Entry DOI: 10.2210/pdb1wcn/pdb
• Related: 1U9L 1WCL
• Descriptor: TRANSCRIPTION ELONGATION PROTEIN NUSA (1 entity in total)
• Functional Keywords: 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
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 1
• Total formula weight: 7469.27

Authors

Eisenmann, A.,Schwarz, S.,Schweimer, K.,Roesch, P. (deposition date: 2004-11-18, release date: 2005-08-31, Last modification date: 2024-05-15)

Primary citation

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

Experimental method

SOLUTION NMR