1wap: Difference between revisions

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

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

caption="1wap, resolution 1.8Å" />

'''TRP RNA-BINDING ATTENUATION PROTEIN IN COMPLEX WITH L-TRYPTOPHAN'''<br />

==Overview==

The crystal structure of the trp RNA-binding attenuation protein of, Bacclius subtilis solved at 1.8 A resolution reveals a novel structural, arrangement in which the eleven subunits are stabilized through eleven, intersubunit beta-sheets to form a beta-wheel with a large central hole., The nature of the binding of L-tryptophan in clefts between adjacent, beta-sheets in the beta-wheel suggests that this binding induces, conformational changes in the flexible residues 25-33 and 49-52. It is, argued that upon binding, the messenger RNA target forms a matching circle, in which eleven U/GAG repeats are bound to the surface of the protein, ondecamer modified by the binding of L-tryptophan.

The crystal structure of the trp RNA-binding attenuation protein of Bacclius subtilis solved at 1.8 A resolution reveals a novel structural arrangement in which the eleven subunits are stabilized through eleven intersubunit beta-sheets to form a beta-wheel with a large central hole. The nature of the binding of L-tryptophan in clefts between adjacent beta-sheets in the beta-wheel suggests that this binding induces conformational changes in the flexible residues 25-33 and 49-52. It is argued that upon binding, the messenger RNA target forms a matching circle in which eleven U/GAG repeats are bound to the surface of the protein ondecamer modified by the binding of L-tryptophan.

==About this Structure==

1WAP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with TRP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1WAP OCA].

1WAP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=TRP:'>TRP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WAP OCA].

==Reference==

Line 13:

[[Category: Bacillus subtilis]]

[[Category: Single protein]]

[[Category: Antson, A.A.]]

[[Category: Antson, A A.]]

[[Category: Dodson, E.J.]]

[[Category: Dodson, E J.]]

[[Category: Gollnick, P.]]

[[Category: TRP]]

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[[Category: trp operon]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:42:16 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1wap.jpg|left|200px]]<br /><applet load="1wap" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1wap.jpg|left|200px]]<br /><applet load="1wap" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1wap, resolution 1.8&Aring;" />
 '''TRP RNA-BINDING ATTENUATION PROTEIN IN COMPLEX WITH L-TRYPTOPHAN'''<br />
 ==Overview==
-The crystal structure of the trp RNA-binding attenuation protein of, Bacclius subtilis solved at 1.8 A resolution reveals a novel structural, arrangement in which the eleven subunits are stabilized through eleven, intersubunit beta-sheets to form a beta-wheel with a large central hole., The nature of the binding of L-tryptophan in clefts between adjacent, beta-sheets in the beta-wheel suggests that this binding induces, conformational changes in the flexible residues 25-33 and 49-52. It is, argued that upon binding, the messenger RNA target forms a matching circle, in which eleven U/GAG repeats are bound to the surface of the protein, ondecamer modified by the binding of L-tryptophan.
+The crystal structure of the trp RNA-binding attenuation protein of Bacclius subtilis solved at 1.8 A resolution reveals a novel structural arrangement in which the eleven subunits are stabilized through eleven intersubunit beta-sheets to form a beta-wheel with a large central hole. The nature of the binding of L-tryptophan in clefts between adjacent beta-sheets in the beta-wheel suggests that this binding induces conformational changes in the flexible residues 25-33 and 49-52. It is argued that upon binding, the messenger RNA target forms a matching circle in which eleven U/GAG repeats are bound to the surface of the protein ondecamer modified by the binding of L-tryptophan.
 ==About this Structure==
-WAP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with TRP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WAP OCA].
+WAP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=TRP:'>TRP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WAP OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Bacillus subtilis]]
 [[Category: Single protein]]
-[[Category: Antson, A.A.]]
+[[Category: Antson, A A.]]
-[[Category: Dodson, E.J.]]
+[[Category: Dodson, E J.]]
 [[Category: Gollnick, P.]]
 [[Category: TRP]]
@@ Line 20: / Line 20: @@
 [[Category: trp operon]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:17:00 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:42:16 2008''