1jfi: Difference between revisions
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== | ==Crystal Structure of the NC2-TBP-DNA Ternary Complex== | ||
<StructureSection load='1jfi' size='340' side='right'caption='[[1jfi]], [[Resolution|resolution]] 2.62Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1jfi]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The July 2005 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''TATA-Binding Protein'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2005_7 10.2210/rcsb_pdb/mom_2005_7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JFI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JFI 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]] 2.62Å</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=1jfi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jfi OCA], [https://pdbe.org/1jfi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jfi RCSB], [https://www.ebi.ac.uk/pdbsum/1jfi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jfi ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1jfi TOPSAN]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/NC2A_HUMAN NC2A_HUMAN] The association of the DR1/DRAP1 heterodimer with TBP results in a functional repression of both activated and basal transcription of class II genes. This interaction precludes the formation of a transcription-competent complex by inhibiting the association of TFIIA and/or TFIIB with TBP. Can bind to DNA on its own.<ref>PMID:8670811</ref> <ref>PMID:8608938</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jf/1jfi_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jfi ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The X-ray structure of a ternary complex of Negative Cofactor 2 (NC2), the TATA box binding protein (TBP), and DNA has been determined at 2.6 A resolution. The N termini of NC2 alpha and beta resemble histones H2A and H2B, respectively, and form a heterodimer that binds to the bent DNA double helix on the underside of the preformed TBP-DNA complex via electrostatic interactions. NC2beta contributes to inhibition of TATA-dependent transcription through interactions of its C-terminal alpha helix with a conserved hydrophobic feature on the upper surface of TBP, which in turn positions the penultimate alpha helix of NC2beta to block recognition of the TBP-DNA complex by transcription factor IIB. Further regulatory implications of the NC2 heterodimer structure are discussed. | The X-ray structure of a ternary complex of Negative Cofactor 2 (NC2), the TATA box binding protein (TBP), and DNA has been determined at 2.6 A resolution. The N termini of NC2 alpha and beta resemble histones H2A and H2B, respectively, and form a heterodimer that binds to the bent DNA double helix on the underside of the preformed TBP-DNA complex via electrostatic interactions. NC2beta contributes to inhibition of TATA-dependent transcription through interactions of its C-terminal alpha helix with a conserved hydrophobic feature on the upper surface of TBP, which in turn positions the penultimate alpha helix of NC2beta to block recognition of the TBP-DNA complex by transcription factor IIB. Further regulatory implications of the NC2 heterodimer structure are discussed. | ||
Crystal structure of negative cofactor 2 recognizing the TBP-DNA transcription complex.,Kamada K, Shu F, Chen H, Malik S, Stelzer G, Roeder RG, Meisterernst M, Burley SK Cell. 2001 Jul 13;106(1):71-81. PMID:11461703<ref>PMID:11461703</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1jfi" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[TATA-binding protein 3D structures|TATA-binding protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: RCSB PDB Molecule of the Month]] | |||
[[Category: TATA-Binding Protein]] | [[Category: TATA-Binding Protein]] | ||
[[Category: Burley | [[Category: Burley SK]] | ||
[[Category: Chen | [[Category: Chen H]] | ||
[[Category: Kamada | [[Category: Kamada K]] | ||
[[Category: Malik | [[Category: Malik S]] | ||
[[Category: Meisterernst | [[Category: Meisterernst M]] | ||
[[Category: Roeder RG]] | |||
[[Category: Roeder | [[Category: Shu F]] | ||
[[Category: Shu | [[Category: Stelzer G]] | ||
[[Category: Stelzer | |||
Latest revision as of 03:44, 6 June 2025
Crystal Structure of the NC2-TBP-DNA Ternary Complex
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