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6NJQ

Structure of TBP-Hoogsteen containing DNA complex

Summary for 6NJQ
Entry DOI10.2210/pdb6njq/pdb
DescriptorTATA-box-binding protein 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 Keywordstbp, hoogsteen, protein-dna, dna binding protein, dna binding protein-dna complex, dna binding protein/dna
Biological sourceArabidopsis thaliana (Mouse-ear cress)
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Total number of polymer chains6
Total formula weight66264.64
Authors
Schumacher, M.A.,Stelling, A. (deposition date: 2019-01-04, release date: 2019-10-30, Last modification date: 2023-10-11)
Primary citationStelling, A.L.,Liu, A.Y.,Zeng, W.,Salinas, R.,Schumacher, M.A.,Al-Hashimi, H.M.
Infrared Spectroscopic Observation of a G-C+Hoogsteen Base Pair in the DNA:TATA-Box Binding Protein Complex Under Solution Conditions.
Angew.Chem.Int.Ed.Engl., 58:12010-12013, 2019
Cited by
PubMed Abstract: Hoogsteen DNA base pairs (bps) are an alternative base pairing to canonical Watson-Crick bps and are thought to play important biochemical roles. Hoogsteen bps have been reported in a handful of X-ray structures of protein-DNA complexes. However, there are several examples of Hoogsteen bps in crystal structures that form Watson-Crick bps when examined under solution conditions. Furthermore, Hoogsteen bps can sometimes be difficult to resolve in DNA:protein complexes by X-ray crystallography due to ambiguous electron density and by solution-state NMR spectroscopy due to size limitations. Here, using infrared spectroscopy, we report the first direct solution-state observation of a Hoogsteen (G-C ) bp in a DNA:protein complex under solution conditions with specific application to DNA-bound TATA-box binding protein. These results support a previous assignment of a G-C Hoogsteen bp in the complex, and indicate that Hoogsteen bps do indeed exist under solution conditions in DNA:protein complexes.
PubMed: 31268220
DOI: 10.1002/anie.201902693
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.75 Å)
Structure validation

227561

数据于2024-11-20公开中

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