1wcn: Difference between revisions

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[[Image:1wcn.gif|left|200px]]<br /><applet load="1wcn" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1wcn.gif|left|200px]]<br /><applet load="1wcn" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1wcn" />

'''NMR STRUCTURE OF THE CARBOXYTERMINAL DOMAINS OF ESCHERICHIA COLI NUSA'''<br />

==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.

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==

1WCN 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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1WCN OCA].

1WCN 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=1WCN OCA].

==Reference==

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[[Category: transcription regulation]]

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@@ Line 1: / Line 1: @@
-[[Image:1wcn.gif|left|200px]]<br /><applet load="1wcn" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1wcn.gif|left|200px]]<br /><applet load="1wcn" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1wcn" />
 '''NMR STRUCTURE OF THE CARBOXYTERMINAL DOMAINS OF ESCHERICHIA COLI NUSA'''<br />
 ==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.
+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==
-WCN 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WCN OCA].
+WCN 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=1WCN OCA].
 ==Reference==
@@ Line 25: / Line 25: @@
 [[Category: transcription regulation]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:18:37 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:42:51 2008''