1wcl

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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wcl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wcl OCA], [http://www.ebi.ac.uk/pdbsum/1wcl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wcl RCSB]</span>
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'''NMR STRUCTURE OF THE CARBOXYTERMINAL DOMAINS OF ESCHERICHIA COLI NUSA'''
'''NMR STRUCTURE OF THE CARBOXYTERMINAL DOMAINS OF ESCHERICHIA COLI NUSA'''
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[[Category: Schwarz, S.]]
[[Category: Schwarz, S.]]
[[Category: Schweimer, K.]]
[[Category: Schweimer, K.]]
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[[Category: c-terminal repeat unit]]
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[[Category: C-terminal repeat unit]]
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[[Category: escherichia coli nusa]]
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[[Category: Escherichia coli nusa]]
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[[Category: nmr]]
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[[Category: Nmr]]
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[[Category: regulation of rna binding]]
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[[Category: Regulation of rna binding]]
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[[Category: transcription antitermination and termination]]
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[[Category: Transcription antitermination and termination]]
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[[Category: transcription regulation]]
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[[Category: Transcription regulation]]
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Revision as of 10:28, 3 May 2008

Template:STRUCTURE 1wcl

NMR STRUCTURE OF THE CARBOXYTERMINAL DOMAINS OF ESCHERICHIA COLI NUSA


Overview

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.

About this Structure

1WCL is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The E. coli NusA carboxy-terminal domains are structurally similar and show specific RNAP- and lambdaN interaction., Eisenmann A, Schwarz S, Prasch S, Schweimer K, Rosch P, Protein Sci. 2005 Aug;14(8):2018-29. Epub 2005 Jun 29. PMID:15987884 Page seeded by OCA on Sat May 3 13:28:07 2008

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