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1wap
From Proteopedia
(New page: 200px<br /><applet load="1wap" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wap, resolution 1.8Å" /> '''TRP RNA-BINDING ATTEN...) |
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| - | [[Image:1wap.jpg|left|200px]]<br /><applet load="1wap" size=" | + | [[Image:1wap.jpg|left|200px]]<br /><applet load="1wap" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wap, resolution 1.8Å" /> | caption="1wap, resolution 1.8Å" /> | ||
'''TRP RNA-BINDING ATTENUATION PROTEIN IN COMPLEX WITH L-TRYPTOPHAN'''<br /> | '''TRP RNA-BINDING ATTENUATION PROTEIN IN COMPLEX WITH L-TRYPTOPHAN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the trp RNA-binding attenuation protein of | + | 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== | ==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:// | + | 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== | ==Reference== | ||
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[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Antson, A | + | [[Category: Antson, A A.]] |
| - | [[Category: Dodson, E | + | [[Category: Dodson, E J.]] |
[[Category: Gollnick, P.]] | [[Category: Gollnick, P.]] | ||
[[Category: TRP]] | [[Category: TRP]] | ||
| Line 20: | Line 20: | ||
[[Category: trp operon]] | [[Category: trp operon]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:42:16 2008'' |
Revision as of 13:42, 21 February 2008
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TRP RNA-BINDING ATTENUATION PROTEIN IN COMPLEX WITH L-TRYPTOPHAN
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.
About this Structure
1WAP is a Single protein structure of sequence from Bacillus subtilis with as ligand. Full crystallographic information is available from OCA.
Reference
The structure of trp RNA-binding attenuation protein., Antson AA, Otridge J, Brzozowski AM, Dodson EJ, Dodson GG, Wilson KS, Smith TM, Yang M, Kurecki T, Gollnick P, Nature. 1995 Apr 20;374(6524):693-700. PMID:7715723
Page seeded by OCA on Thu Feb 21 15:42:16 2008
