1gtn

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(New page: 200px<br /><applet load="1gtn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gtn, resolution 2.50&Aring;" /> '''STRUCTURE OF THE TRP...)
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[[Image:1gtn.jpg|left|200px]]<br /><applet load="1gtn" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1gtn, resolution 2.50&Aring;" />
caption="1gtn, resolution 2.50&Aring;" />
'''STRUCTURE OF THE TRP RNA-BINDING ATTENUATION PROTEIN (TRAP) BOUND TO AN RNA MOLECULE CONTAINING 11 GAGCC REPEATS'''<br />
'''STRUCTURE OF THE TRP RNA-BINDING ATTENUATION PROTEIN (TRAP) BOUND TO AN RNA MOLECULE CONTAINING 11 GAGCC REPEATS'''<br />
==Overview==
==Overview==
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The trp RNA-binding attenuation protein (TRAP) regulates expression of the, tryptophan biosynthetic genes in bacilli by binding to the leader region, of the nascent trp operon mRNA. When activated by binding tryptophan, the, 11-subunit circular TRAP molecule binds to a target sequence consisting of, 11 (G/U)AG repeats, separated by two or three variable 'spacer', nucleotides. Reported here are two crystal structures of TRAP bound to, RNAs containing 11 GAG repeats separated by UU and CC spacer nucleotides, determined at 1.75 and 2.50 A resolution, respectively. These show the, spacer regions of the RNA molecules to be highly flexible, making no, direct hydrogen-bonding contacts with the protein. Comparison of these, structures with the previous structure of TRAP bound to (GAGAU)(10)GAG, RNA, in which the spacer nucleotides stack with each other close to the, protein surface, shows that the RNA can adopt different conformations, depending on the sequence of the spacer regions. This gives insight into, the structural basis of the specificity of TRAP and into the mechanism of, binding.
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The trp RNA-binding attenuation protein (TRAP) regulates expression of the tryptophan biosynthetic genes in bacilli by binding to the leader region of the nascent trp operon mRNA. When activated by binding tryptophan, the 11-subunit circular TRAP molecule binds to a target sequence consisting of 11 (G/U)AG repeats, separated by two or three variable 'spacer' nucleotides. Reported here are two crystal structures of TRAP bound to RNAs containing 11 GAG repeats separated by UU and CC spacer nucleotides, determined at 1.75 and 2.50 A resolution, respectively. These show the spacer regions of the RNA molecules to be highly flexible, making no direct hydrogen-bonding contacts with the protein. Comparison of these structures with the previous structure of TRAP bound to (GAGAU)(10)GAG RNA, in which the spacer nucleotides stack with each other close to the protein surface, shows that the RNA can adopt different conformations depending on the sequence of the spacer regions. This gives insight into the structural basis of the specificity of TRAP and into the mechanism of binding.
==About this Structure==
==About this Structure==
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1GTN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with TRP and TRP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GTN OCA].
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1GTN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with <scene name='pdbligand=TRP:'>TRP</scene> and <scene name='pdbligand=TRP:'>TRP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GTN OCA].
==Reference==
==Reference==
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[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Antson, A.A.]]
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[[Category: Antson, A A.]]
[[Category: Gollnick, P.]]
[[Category: Gollnick, P.]]
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[[Category: Hopcroft, N.H.]]
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[[Category: Hopcroft, N H.]]
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[[Category: Wendt, A.L.]]
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[[Category: Wendt, A L.]]
[[Category: TRP]]
[[Category: TRP]]
[[Category: rna-binding protein]]
[[Category: rna-binding protein]]
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[[Category: trp rna]]
[[Category: trp rna]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:17:01 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:53:48 2008''

Revision as of 10:53, 21 February 2008


1gtn, resolution 2.50Å

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STRUCTURE OF THE TRP RNA-BINDING ATTENUATION PROTEIN (TRAP) BOUND TO AN RNA MOLECULE CONTAINING 11 GAGCC REPEATS

Overview

The trp RNA-binding attenuation protein (TRAP) regulates expression of the tryptophan biosynthetic genes in bacilli by binding to the leader region of the nascent trp operon mRNA. When activated by binding tryptophan, the 11-subunit circular TRAP molecule binds to a target sequence consisting of 11 (G/U)AG repeats, separated by two or three variable 'spacer' nucleotides. Reported here are two crystal structures of TRAP bound to RNAs containing 11 GAG repeats separated by UU and CC spacer nucleotides, determined at 1.75 and 2.50 A resolution, respectively. These show the spacer regions of the RNA molecules to be highly flexible, making no direct hydrogen-bonding contacts with the protein. Comparison of these structures with the previous structure of TRAP bound to (GAGAU)(10)GAG RNA, in which the spacer nucleotides stack with each other close to the protein surface, shows that the RNA can adopt different conformations depending on the sequence of the spacer regions. This gives insight into the structural basis of the specificity of TRAP and into the mechanism of binding.

About this Structure

1GTN is a Protein complex structure of sequences from Geobacillus stearothermophilus with and as ligands. Full crystallographic information is available from OCA.

Reference

Specificity of TRAP-RNA interactions: crystal structures of two complexes with different RNA sequences., Hopcroft NH, Wendt AL, Gollnick P, Antson AA, Acta Crystallogr D Biol Crystallogr. 2002 Apr;58(Pt 4):615-21. Epub 2002, Mar 22. PMID:11914485

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