1C9B

CRYSTAL STRUCTURE OF A HUMAN TBP CORE DOMAIN-HUMAN TFIIB CORE DOMAIN COMPLEX BOUND TO AN EXTENDED, MODIFIED ADENOVIRAL MAJOR LATE PROMOTER (ADMLP)

Summary for 1C9B

• Entry DOI: 10.2210/pdb1c9b/pdb
• Related: 1AIS 1TFB 1VOL
• Descriptor: ADMLP TATA-BOX DNA CONTAINING IIB RECOGNITION ELEMENT, GENERAL TRANSCRIPTION FACTOR IIB, TATA BOX BINDING PROTEIN, ... (5 entities in total)
• Functional Keywords: protein-dna complex, cyclin-like fold, helix-turn-helix, tata-box, transcription-dna complex, transcription/dna
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: Q00403 P20226
• Total number of polymer chains: 20
• Total formula weight: 272215.83

Authors

Tsai, F.T.F.,Sigler, P.B. (deposition date: 1999-08-01, release date: 2000-01-10, Last modification date: 2024-02-07)

Primary citation

Tsai, F.T.,Sigler, P.B.
Structural basis of preinitiation complex assembly on human pol II promoters.
EMBO J., 19:25-36, 2000

PubMed Abstract: Transcription initiation requires the assembly of a preinitiation complex (PIC), which is nucleated through binding of the TATA-box binding protein (TBP) to the promoter. Biochemical studies have shown, however, that TBP recognizes the TATA-box in both orientations and, therefore, cannot account for the directionality of PIC assembly. Transcription factor IIB (TFIIB) is essential for transcription initiation from RNA polymerase II promoters. Recent functional studies have identified a specific 7 bp TFIIB recognition element (BRE) immediately upstream of the TATA-box. We present here the 2.65 A resolution crystal structure of a human TFIIBc-TBPc complex bound to an idealized and extended adenovirus major late promoter. This structure now reveals that human TFIIBc binds to the promoter asymmetrically through base-specific contacts in the major groove upstream and in the minor groove downstream of the TATA-box. Binding of TFIIBc is, therefore, synergistic with TBPc requiring the distortion of the TATA-box. Thus, the newly described TFIIBc-DNA interface is likely to be a key determinant for the unidirectional assembly of a functional PIC.

PubMed: 10619841
DOI: 10.1093/emboj/19.1.25

Experimental method

X-RAY DIFFRACTION (2.65 Å)