1qn8: Difference between revisions

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New page: left|200px<br /><applet load="1qn8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qn8, resolution 2.1Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1qn8.gif|left|200px]]<br /><applet load="1qn8" size="450" color="white" frame="true" align="right" spinBox="true"  
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caption="1qn8, resolution 2.1&Aring;" />
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'''CRYSTAL STRUCTURE OF THE T(-28) ADENOVIRUS MAJOR LATE PROMOTER TATA BOX VARIANT BOUND TO WILD-TYPE TBP (ARABIDOPSIS THALIANA TBP ISOFORM 2). TATA ELEMENT RECOGNITION BY THE TATA BOX-BINDING PROTEIN HAS BEEN CONSERVED THROUGHOUT EVOLUTION'''<br />
'''CRYSTAL STRUCTURE OF THE T(-28) ADENOVIRUS MAJOR LATE PROMOTER TATA BOX VARIANT BOUND TO WILD-TYPE TBP (ARABIDOPSIS THALIANA TBP ISOFORM 2). TATA ELEMENT RECOGNITION BY THE TATA BOX-BINDING PROTEIN HAS BEEN CONSERVED THROUGHOUT EVOLUTION'''<br />


==Overview==
==Overview==
Cocrystal structures of wild-type TATA box-binding protein (TBP), recognizing 10 naturally occurring TATA elements have been determined at, 2.3-1.8 A resolution, and compared with our 1.9 A resolution structure of, TBP bound to the Adenovirus major late promoter (AdMLP) TATA box, (5'-TATAAAAG-3'). Minor-groove recognition by the saddle-shaped protein, induces the same conformational change in each of these oligonucleotides, despite variations in promoter sequence that reduce the efficiency of, transcription initiation. Three molecular mechanisms explain assembly of, diverse TBP-TATA element complexes. (1) T --&gt; A and A --&gt; T transversions, leave the minor-groove face unchanged, permitting formation of TBP-DNA, complexes on many A/T-rich core promoter sequences. (2) Cavities in the, interface between TBP and the minor-groove face of the AdMLP TATA box, accommodate the exocyclic NH(2) groups of G in a TACA box and in a TATAAG, box. (3) Formation of a C:G Hoogsteen basepair in a TATAAAC box eliminates, steric clashes that would be produced by the Watson-Crick base pair. We, conclude that the structure of the TBP-TATA box complex found at the heart, of the polymerase II (pol II) transcription machinery has remained, constant over the course of evolution, despite variations in TBP and its, DNA targets.
Cocrystal structures of wild-type TATA box-binding protein (TBP) recognizing 10 naturally occurring TATA elements have been determined at 2.3-1.8 A resolution, and compared with our 1.9 A resolution structure of TBP bound to the Adenovirus major late promoter (AdMLP) TATA box (5'-TATAAAAG-3'). Minor-groove recognition by the saddle-shaped protein induces the same conformational change in each of these oligonucleotides, despite variations in promoter sequence that reduce the efficiency of transcription initiation. Three molecular mechanisms explain assembly of diverse TBP-TATA element complexes. (1) T --&gt; A and A --&gt; T transversions leave the minor-groove face unchanged, permitting formation of TBP-DNA complexes on many A/T-rich core promoter sequences. (2) Cavities in the interface between TBP and the minor-groove face of the AdMLP TATA box accommodate the exocyclic NH(2) groups of G in a TACA box and in a TATAAG box. (3) Formation of a C:G Hoogsteen basepair in a TATAAAC box eliminates steric clashes that would be produced by the Watson-Crick base pair. We conclude that the structure of the TBP-TATA box complex found at the heart of the polymerase II (pol II) transcription machinery has remained constant over the course of evolution, despite variations in TBP and its DNA targets.


==About this Structure==
==About this Structure==
1QN8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QN8 OCA].  
1QN8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QN8 OCA].  


==Reference==
==Reference==
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[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Burley, S.K.]]
[[Category: Burley, S K.]]
[[Category: Kim, J.L.]]
[[Category: Kim, J L.]]
[[Category: Kodadek, T.]]
[[Category: Kodadek, T.]]
[[Category: Patikoglou, G.A.]]
[[Category: Patikoglou, G A.]]
[[Category: Sun, L.]]
[[Category: Sun, L.]]
[[Category: Yang, S.H.]]
[[Category: Yang, S H.]]
[[Category: adenovirus major late promoter (admlp) tata box]]
[[Category: adenovirus major late promoter (admlp) tata box]]
[[Category: t (-28) tata box variant]]
[[Category: t (-28) tata box variant]]
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[[Category: tbp-tata element complexes]]
[[Category: tbp-tata element complexes]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:41:35 2008''

Revision as of 15:41, 21 February 2008

File:1qn8.gif


1qn8, resolution 2.1Å

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CRYSTAL STRUCTURE OF THE T(-28) ADENOVIRUS MAJOR LATE PROMOTER TATA BOX VARIANT BOUND TO WILD-TYPE TBP (ARABIDOPSIS THALIANA TBP ISOFORM 2). TATA ELEMENT RECOGNITION BY THE TATA BOX-BINDING PROTEIN HAS BEEN CONSERVED THROUGHOUT EVOLUTION

OverviewOverview

Cocrystal structures of wild-type TATA box-binding protein (TBP) recognizing 10 naturally occurring TATA elements have been determined at 2.3-1.8 A resolution, and compared with our 1.9 A resolution structure of TBP bound to the Adenovirus major late promoter (AdMLP) TATA box (5'-TATAAAAG-3'). Minor-groove recognition by the saddle-shaped protein induces the same conformational change in each of these oligonucleotides, despite variations in promoter sequence that reduce the efficiency of transcription initiation. Three molecular mechanisms explain assembly of diverse TBP-TATA element complexes. (1) T --> A and A --> T transversions leave the minor-groove face unchanged, permitting formation of TBP-DNA complexes on many A/T-rich core promoter sequences. (2) Cavities in the interface between TBP and the minor-groove face of the AdMLP TATA box accommodate the exocyclic NH(2) groups of G in a TACA box and in a TATAAG box. (3) Formation of a C:G Hoogsteen basepair in a TATAAAC box eliminates steric clashes that would be produced by the Watson-Crick base pair. We conclude that the structure of the TBP-TATA box complex found at the heart of the polymerase II (pol II) transcription machinery has remained constant over the course of evolution, despite variations in TBP and its DNA targets.

About this StructureAbout this Structure

1QN8 is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

ReferenceReference

TATA element recognition by the TATA box-binding protein has been conserved throughout evolution., Patikoglou GA, Kim JL, Sun L, Yang SH, Kodadek T, Burley SK, Genes Dev. 1999 Dec 15;13(24):3217-30. PMID:10617571

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