1vok
From Proteopedia
(New page: 200px<br /><applet load="1vok" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vok, resolution 2.1Å" /> '''ARABIDOPSIS THALIANA ...) |
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| - | [[Image:1vok.jpg|left|200px]]<br /><applet load="1vok" size=" | + | [[Image:1vok.jpg|left|200px]]<br /><applet load="1vok" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1vok, resolution 2.1Å" /> | caption="1vok, resolution 2.1Å" /> | ||
'''ARABIDOPSIS THALIANA TBP (DIMER)'''<br /> | '''ARABIDOPSIS THALIANA TBP (DIMER)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of a TATA box-binding protein (TBP2) from | + | The three-dimensional structure of a TATA box-binding protein (TBP2) from Arabidopsis thaliana has been refined at 2.1 A resolution. TBPs are general eukaryotic transcription factors that participate in initiation of RNA synthesis by all three eukaryotic RNA polymerases. The carboxy-terminal portion of TBP is a unique DNA-binding motif/protein fold, adopting a highly symmetric alpha/beta structure that resembles a molecular saddle with two stirrup-like loops. A ten-stranded, antiparallel beta-sheet provides a concave surface for recognizing class II nuclear gene promoters, while the four amphipathic alpha-helices on the convex surface are available for interaction with other transcription factors. The myriad interactions of TBP2 with components of the transcription machinery are discussed. |
==About this Structure== | ==About this Structure== | ||
| - | 1VOK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1VOK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VOK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Burley, S | + | [[Category: Burley, S K.]] |
| - | [[Category: Nikolov, D | + | [[Category: Nikolov, D B.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: dna binding]] | [[Category: dna binding]] | ||
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[[Category: transcription initiation]] | [[Category: transcription initiation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:36:58 2008'' |
Revision as of 13:37, 21 February 2008
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ARABIDOPSIS THALIANA TBP (DIMER)
Overview
The three-dimensional structure of a TATA box-binding protein (TBP2) from Arabidopsis thaliana has been refined at 2.1 A resolution. TBPs are general eukaryotic transcription factors that participate in initiation of RNA synthesis by all three eukaryotic RNA polymerases. The carboxy-terminal portion of TBP is a unique DNA-binding motif/protein fold, adopting a highly symmetric alpha/beta structure that resembles a molecular saddle with two stirrup-like loops. A ten-stranded, antiparallel beta-sheet provides a concave surface for recognizing class II nuclear gene promoters, while the four amphipathic alpha-helices on the convex surface are available for interaction with other transcription factors. The myriad interactions of TBP2 with components of the transcription machinery are discussed.
About this Structure
1VOK is a Single protein structure of sequence from Arabidopsis thaliana with as ligand. Full crystallographic information is available from OCA.
Reference
2.1 A resolution refined structure of a TATA box-binding protein (TBP)., Nikolov DB, Burley SK, Nat Struct Biol. 1994 Sep;1(9):621-37. PMID:7634102
Page seeded by OCA on Thu Feb 21 15:36:58 2008
