1wcl
From Proteopedia
(New page: 200px<br /><applet load="1wcl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wcl" /> '''NMR STRUCTURE OF THE CARBOXYTERMINAL DOMAINS...) |
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| - | [[Image:1wcl.gif|left|200px]]<br /><applet load="1wcl" size=" | + | [[Image:1wcl.gif|left|200px]]<br /><applet load="1wcl" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wcl" /> | caption="1wcl" /> | ||
'''NMR STRUCTURE OF THE CARBOXYTERMINAL DOMAINS OF ESCHERICHIA COLI NUSA'''<br /> | '''NMR STRUCTURE OF THE CARBOXYTERMINAL DOMAINS OF ESCHERICHIA COLI NUSA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The carboxy-terminal domain of the transcription factor Escherichia coli | + | 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== | ==About this Structure== | ||
| - | 1WCL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1WCL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WCL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:42:53 2008'' |
Revision as of 13:42, 21 February 2008
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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
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