1wrt: Difference between revisions

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

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

caption="1wrt" />

'''NMR STUDY OF APO TRP REPRESSOR'''<br />

==Overview==

The solution structures of the trp-repressor from Escherichia coli in both, the liganded (holo-) and unliganded (apo-) form, have been refined by, restrained molecular dynamics with simulated annealing using the program, XPLOR and additional experimental constraints. The ensemble of refined, holorepressor structures have a root-mean-square deviation (r.m.s.d.) of, 0.8 A relative to the average structure for the backbone of the dimer core, (helices A, B, C, A', B', C') and 2.5 A for the helix-turn-helix, DNA-binding domain (helices D and E). The corresponding values for the, aporepressor are 0.9 A for the backbone of the ABC-dimer core and 3.2 A, for the DE helix-turn-helix. The r.m.s.d. of the average structures from, the corresponding crystal structures are 2.3 A for the holorepressor ABC, core and 4.2 A for its DE region; 2.3 A for the aporepressor core and 5.5, A for its DE region. The relative disorder of the DNA-binding domain is, reflected in a number of experimental parameters including substantially, more rapid backbone proton exchange rates, exchange-limited relaxation, times and crystallographic B-factors. The stabilizing effect of the L-Trp, ligand is evident in these measurements, as it is in the higher precision, of the holorepressor structure.

The solution structures of the trp-repressor from Escherichia coli in both the liganded (holo-) and unliganded (apo-) form, have been refined by restrained molecular dynamics with simulated annealing using the program XPLOR and additional experimental constraints. The ensemble of refined holorepressor structures have a root-mean-square deviation (r.m.s.d.) of 0.8 A relative to the average structure for the backbone of the dimer core (helices A, B, C, A', B', C') and 2.5 A for the helix-turn-helix DNA-binding domain (helices D and E). The corresponding values for the aporepressor are 0.9 A for the backbone of the ABC-dimer core and 3.2 A for the DE helix-turn-helix. The r.m.s.d. of the average structures from the corresponding crystal structures are 2.3 A for the holorepressor ABC core and 4.2 A for its DE region; 2.3 A for the aporepressor core and 5.5 A for its DE region. The relative disorder of the DNA-binding domain is reflected in a number of experimental parameters including substantially more rapid backbone proton exchange rates, exchange-limited relaxation times and crystallographic B-factors. The stabilizing effect of the L-Trp ligand is evident in these measurements, as it is in the higher precision of the holorepressor structure.

==About this Structure==

1WRT 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=1WRT OCA].

1WRT 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=1WRT OCA].

==Reference==

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[[Category: transcription regulation]]

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@@ Line 1: / Line 1: @@
-[[Image:1wrt.gif|left|200px]]<br /><applet load="1wrt" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1wrt.gif|left|200px]]<br /><applet load="1wrt" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1wrt" />
 '''NMR STUDY OF APO TRP REPRESSOR'''<br />
 ==Overview==
-The solution structures of the trp-repressor from Escherichia coli in both, the liganded (holo-) and unliganded (apo-) form, have been refined by, restrained molecular dynamics with simulated annealing using the program, XPLOR and additional experimental constraints. The ensemble of refined, holorepressor structures have a root-mean-square deviation (r.m.s.d.) of, 0.8 A relative to the average structure for the backbone of the dimer core, (helices A, B, C, A', B', C') and 2.5 A for the helix-turn-helix, DNA-binding domain (helices D and E). The corresponding values for the, aporepressor are 0.9 A for the backbone of the ABC-dimer core and 3.2 A, for the DE helix-turn-helix. The r.m.s.d. of the average structures from, the corresponding crystal structures are 2.3 A for the holorepressor ABC, core and 4.2 A for its DE region; 2.3 A for the aporepressor core and 5.5, A for its DE region. The relative disorder of the DNA-binding domain is, reflected in a number of experimental parameters including substantially, more rapid backbone proton exchange rates, exchange-limited relaxation, times and crystallographic B-factors. The stabilizing effect of the L-Trp, ligand is evident in these measurements, as it is in the higher precision, of the holorepressor structure.
+The solution structures of the trp-repressor from Escherichia coli in both the liganded (holo-) and unliganded (apo-) form, have been refined by restrained molecular dynamics with simulated annealing using the program XPLOR and additional experimental constraints. The ensemble of refined holorepressor structures have a root-mean-square deviation (r.m.s.d.) of 0.8 A relative to the average structure for the backbone of the dimer core (helices A, B, C, A', B', C') and 2.5 A for the helix-turn-helix DNA-binding domain (helices D and E). The corresponding values for the aporepressor are 0.9 A for the backbone of the ABC-dimer core and 3.2 A for the DE helix-turn-helix. The r.m.s.d. of the average structures from the corresponding crystal structures are 2.3 A for the holorepressor ABC core and 4.2 A for its DE region; 2.3 A for the aporepressor core and 5.5 A for its DE region. The relative disorder of the DNA-binding domain is reflected in a number of experimental parameters including substantially more rapid backbone proton exchange rates, exchange-limited relaxation times and crystallographic B-factors. The stabilizing effect of the L-Trp ligand is evident in these measurements, as it is in the higher precision of the holorepressor structure.
 ==About this Structure==
-WRT 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=1WRT OCA].
+WRT 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=1WRT OCA].
 ==Reference==
@@ Line 19: / Line 19: @@
 [[Category: transcription regulation]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:37:50 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:47:27 2008''