1R5U

RNA POLYMERASE II TFIIB COMPLEX

Summary for 1R5U

• Entry DOI: 10.2210/pdb1r5u/pdb
• Related: 1I3q 1I5o 1I6h 1NIK 1dl6 1pft
• Descriptor: DNA-directed RNA polymerase II largest subunit, DNA-directed RNA polymerases I, II, and III 7.7 kDa polypeptide, TRANSCRIPTION FACTOR II B (TFIIB), ... (13 entities in total)
• Functional Keywords: zinc ribbon, transcription
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Nucleus: P04050 P08518 P16370 P20434 P20436 P27999 P38902; Nucleus, nucleolus: P40422 P22139; Cytoplasm: P20435
• Total number of polymer chains: 11
• Total formula weight: 477576.00

Authors

Bushnell, D.A.,Westover, K.D.,Davis, R.,Kornberg, R.D. (deposition date: 2003-10-13, release date: 2004-02-17, Last modification date: 2023-08-23)

Primary citation

Bushnell, D.A.,Westover, K.D.,Davis, R.E.,Kornberg, R.D.
Structural basis of transcription: an RNA polymerase II-TFIIB cocrystal at 4.5 Angstroms.
Science, 303:983-988, 2004

PubMed Abstract: The structure of the general transcription factor IIB (TFIIB) in a complex with RNA polymerase II reveals three features crucial for transcription initiation: an N-terminal zinc ribbon domain of TFIIB that contacts the "dock" domain of the polymerase, near the path of RNA exit from a transcribing enzyme; a "finger" domain of TFIIB that is inserted into the polymerase active center; and a C-terminal domain, whose interaction with both the polymerase and with a TATA box-binding protein (TBP)-promoter DNA complex orients the DNA for unwinding and transcription. TFIIB stabilizes an early initiation complex, containing an incomplete RNA-DNA hybrid region. It may interact with the template strand, which sets the location of the transcription start site, and may interfere with RNA exit, which leads to abortive initiation or promoter escape. The trajectory of promoter DNA determined by the C-terminal domain of TFIIB traverses sites of interaction with TFIIE, TFIIF, and TFIIH, serving to define their roles in the transcription initiation process.

PubMed: 14963322
DOI: 10.1126/science.1090838

Experimental method

X-RAY DIFFRACTION (4.5 Å)