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1JFI

Crystal Structure of the NC2-TBP-DNA Ternary Complex

Summary for 1JFI
Entry DOI10.2210/pdb1jfi/pdb
Descriptor5'-D(*TP*TP*GP*GP*CP*TP*AP*TP*AP*AP*AP*AP*GP*GP*GP*CP*TP*CP*C)-3', 5'-D(*G*GP*AP*GP*CP*CP*CP*TP*TP*TP*TP*AP*TP*AP*GP*CP*CP*AP*A)-3', Transcription Regulator NC2 alpha chain, ... (6 entities in total)
Functional Keywordshistone, h2a/h2b, tbp, tata-dna, transcription initiation, nc2, negative cofactor, structural genomics, psi, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, transcription-dna complex, transcription/dna
Biological sourceHomo sapiens (human)
More
Total number of polymer chains5
Total formula weight63075.92
Authors
Kamada, K.,Shu, F.,Chen, H.,Malik, S.,Stelzer, G.,Roeder, R.G.,Meisterernst, M.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2001-06-20, release date: 2001-07-11, Last modification date: 2023-08-16)
Primary citationKamada, K.,Shu, F.,Chen, H.,Malik, S.,Stelzer, G.,Roeder, R.G.,Meisterernst, M.,Burley, S.K.
Crystal structure of negative cofactor 2 recognizing the TBP-DNA transcription complex.
Cell(Cambridge,Mass.), 106:71-81, 2001
Cited by
PubMed Abstract: 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.
PubMed: 11461703
DOI: 10.1016/S0092-8674(01)00417-2
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.62 Å)
Structure validation

229380

數據於2024-12-25公開中

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