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1QN3

Crystal structure of the C(-25) 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.

Summary for 1QN3
Entry DOI10.2210/pdb1qn3/pdb
Related1QN4 1QN5 1QN6 1QN7 1QN8 1QN9 1QNA 1QNB 1QNC 1QNE
DescriptorTRANSCRIPTION INITIATION FACTOR TFIID-1, DNA (5'-D(*GP*CP*TP*AP*TP*AP*AP*AP*CP*GP*GP*GP*CP*A)-3'), DNA (5'-D(*TP*GP*CP*CP*CP*GP*TP*TP*TP*AP*TP*AP*GP*C)-3'), ... (4 entities in total)
Functional Keywordstata box-binding protein (tbp), adenovirus major late promoter (admlp) tata box, tbp-tata element complex, c(-25) tata box variant
Biological sourceARABIDOPSIS THALIANA (MOUSE-EAR CRESS)
Total number of polymer chains6
Total formula weight61921.90
Authors
Patikoglou, G.A.,Kim, J.L.,Sun, L.,Yang, S.-H.,Kodadek, T.,Burley, S.K. (deposition date: 1999-10-14, release date: 2000-02-06, Last modification date: 2024-05-08)
Primary citationPatikoglou, G.A.,Kim, J.L.,Sun, L.,Yang, S.-H.,Kodadek, T.,Burley, S.K.
TATA Element Recognition by the TATA Box-Binding Protein Has Been Conserved Throughout Evolution
Genes Dev., 13:3217-, 1999
Cited by
PubMed Abstract: 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.
PubMed: 10617571
DOI: 10.1101/GAD.13.24.3217
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.95 Å)
Structure validation

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