1aoy: Difference between revisions

Line 1:

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

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

caption="1aoy" />

'''N-TERMINAL DOMAIN OF ESCHERICHIA COLI ARGININE REPRESSOR NMR, 23 STRUCTURES'''<br />

==Overview==

The structure of the monomeric DNA-binding domain of the Escherichia coli, arginine repressor, ArgR, determined by NMR spectroscopy, shows structural, homology to the winged helix-turn-helix (wHTH) family, a motif found in a, diverse class of proteins including both gene regulators and gene, organizers from prokaryotes and eukaryotes. Biochemical data on DNA, binding by intact ArgR are used as constraints to position the domain on, its DNA target and to derive a model for the hexamer-DNA complex using the, known structure of the L-arginine-binding domain. The structural, independence of the wHTH fold may be important for multimeric DNA-binding, proteins that contact extended DNA regions with imperfect match to, consensus sequences, a feature of many wHTH-domain proteins.

The structure of the monomeric DNA-binding domain of the Escherichia coli arginine repressor, ArgR, determined by NMR spectroscopy, shows structural homology to the winged helix-turn-helix (wHTH) family, a motif found in a diverse class of proteins including both gene regulators and gene organizers from prokaryotes and eukaryotes. Biochemical data on DNA binding by intact ArgR are used as constraints to position the domain on its DNA target and to derive a model for the hexamer-DNA complex using the known structure of the L-arginine-binding domain. The structural independence of the wHTH fold may be important for multimeric DNA-binding proteins that contact extended DNA regions with imperfect match to consensus sequences, a feature of many wHTH-domain proteins.

==About this Structure==

1AOY 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=1AOY OCA].

1AOY 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=1AOY OCA].

==Reference==

Line 21:

[[Category: winged helix]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20~~ 11:00:~~54 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:46:48 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1aoy.jpg|left|200px]]<br /><applet load="1aoy" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1aoy.jpg|left|200px]]<br /><applet load="1aoy" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1aoy" />
 '''N-TERMINAL DOMAIN OF ESCHERICHIA COLI ARGININE REPRESSOR NMR, 23 STRUCTURES'''<br />
 ==Overview==
-The structure of the monomeric DNA-binding domain of the Escherichia coli, arginine repressor, ArgR, determined by NMR spectroscopy, shows structural, homology to the winged helix-turn-helix (wHTH) family, a motif found in a, diverse class of proteins including both gene regulators and gene, organizers from prokaryotes and eukaryotes. Biochemical data on DNA, binding by intact ArgR are used as constraints to position the domain on, its DNA target and to derive a model for the hexamer-DNA complex using the, known structure of the L-arginine-binding domain. The structural, independence of the wHTH fold may be important for multimeric DNA-binding, proteins that contact extended DNA regions with imperfect match to, consensus sequences, a feature of many wHTH-domain proteins.
+The structure of the monomeric DNA-binding domain of the Escherichia coli arginine repressor, ArgR, determined by NMR spectroscopy, shows structural homology to the winged helix-turn-helix (wHTH) family, a motif found in a diverse class of proteins including both gene regulators and gene organizers from prokaryotes and eukaryotes. Biochemical data on DNA binding by intact ArgR are used as constraints to position the domain on its DNA target and to derive a model for the hexamer-DNA complex using the known structure of the L-arginine-binding domain. The structural independence of the wHTH fold may be important for multimeric DNA-binding proteins that contact extended DNA regions with imperfect match to consensus sequences, a feature of many wHTH-domain proteins.
 ==About this Structure==
-AOY 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=1AOY OCA].
+AOY 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=1AOY OCA].
 ==Reference==
@@ Line 21: / Line 21: @@
 [[Category: winged helix]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:00:54 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:46:48 2008''