1vtl: Difference between revisions

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'''Unreleased structure'''


The entry 1vtl is ON HOLD
==CO-CRYSTAL STRUCTURE OF TBP RECOGNIZING THE MINOR GROOVE OF A TATA ELEMENT==
<StructureSection load='1vtl' size='340' side='right'caption='[[1vtl]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1vtl]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VTL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VTL FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vtl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vtl OCA], [https://pdbe.org/1vtl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vtl RCSB], [https://www.ebi.ac.uk/pdbsum/1vtl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vtl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TBP1_ARATH TBP1_ARATH] General transcription factor that functions at the core of the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA box is the initial transcriptional step of the pre-initiation complex (PIC), playing a role in the activation of eukaryotic genes transcribed by RNA polymerase II.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The three-dimensional structure of a TATA-box binding polypeptide complexed with the TATA element of the adenovirus major late promoter has been determined by X-ray crystallography at 2.25 A resolution. Binding of the saddle-shaped protein induces a conformational change in the DNA, inducing sharp kinks at either end of the sequence TATAAAAG. Between the kinks, the right-handed double helix is smoothly curved and partially unwound, presenting a widened minor groove to TBP's concave, antiparallel beta-sheet. Side-chain/base interactions are restricted to the minor groove, and include hydrogen bonds, van der Waals contacts and phenylalanine-base stacking interactions.


Authors: Kim, J.L., Nikolov, D.B., Burley, S.K.
Co-crystal structure of TBP recognizing the minor groove of a TATA element.,Kim JL, Nikolov DB, Burley SK Nature. 1993 Oct 7;365(6446):520-7. PMID:8413605<ref>PMID:8413605</ref>


Description: CO-CRYSTAL STRUCTURE OF TBP RECOGNIZING THE MINOR GROOVE OF A TATA ELEMENT
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1vtl" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[TATA-binding protein 3D structures|TATA-binding protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Burley SK]]
[[Category: Kim JL]]
[[Category: Nikolov DB]]

Latest revision as of 03:06, 28 December 2023

CO-CRYSTAL STRUCTURE OF TBP RECOGNIZING THE MINOR GROOVE OF A TATA ELEMENTCO-CRYSTAL STRUCTURE OF TBP RECOGNIZING THE MINOR GROOVE OF A TATA ELEMENT

Structural highlights

1vtl is a 6 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.25Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TBP1_ARATH General transcription factor that functions at the core of the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA box is the initial transcriptional step of the pre-initiation complex (PIC), playing a role in the activation of eukaryotic genes transcribed by RNA polymerase II.

Publication Abstract from PubMed

The three-dimensional structure of a TATA-box binding polypeptide complexed with the TATA element of the adenovirus major late promoter has been determined by X-ray crystallography at 2.25 A resolution. Binding of the saddle-shaped protein induces a conformational change in the DNA, inducing sharp kinks at either end of the sequence TATAAAAG. Between the kinks, the right-handed double helix is smoothly curved and partially unwound, presenting a widened minor groove to TBP's concave, antiparallel beta-sheet. Side-chain/base interactions are restricted to the minor groove, and include hydrogen bonds, van der Waals contacts and phenylalanine-base stacking interactions.

Co-crystal structure of TBP recognizing the minor groove of a TATA element.,Kim JL, Nikolov DB, Burley SK Nature. 1993 Oct 7;365(6446):520-7. PMID:8413605[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Kim JL, Nikolov DB, Burley SK. Co-crystal structure of TBP recognizing the minor groove of a TATA element. Nature. 1993 Oct 7;365(6446):520-7. PMID:8413605 doi:http://dx.doi.org/10.1038/365520a0

1vtl, resolution 2.25Å

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