1AIS

TATA-BINDING PROTEIN/TRANSCRIPTION FACTOR (II)B/TATA-BOX COMPLEX FROM PYROCOCCUS WOESEI

Summary for 1AIS

• Entry DOI: 10.2210/pdb1ais/pdb
• Descriptor: DNA (5'-D(*AP*AP*CP*TP*TP*AP*CP*TP*TP*TP*(5IU)P*(5IU)P*AP*AP*AP*GP*C)-3'), DNA (5'-D(*GP*CP*TP*TP*TP*AP*AP*AP*AP*AP*GP*TP*AP*AP*GP*TP*T )-3'), PROTEIN (TATA-BINDING PROTEIN), ... (5 entities in total)
• Functional Keywords: transcription, hyperthermophile, ribosome binding, complex (ribosome binding- dna), transcription-dna complex, transcription/dna
• Biological source: Pyrococcus woesei; More
• Total number of polymer chains: 4
• Total formula weight: 53503.66

Authors

Kosa, P.F.,Ghosh, G.,Dedecker, B.S.,Sigler, P.B. (deposition date: 1997-04-24, release date: 1997-07-07, Last modification date: 2011-07-13)

Primary citation

Kosa, P.F.,Ghosh, G.,DeDecker, B.S.,Sigler, P.B.
The 2.1-A crystal structure of an archaeal preinitiation complex: TATA-box-binding protein/transcription factor (II)B core/TATA-box.
Proc.Natl.Acad.Sci.USA, 94:6042-6047, 1997

PubMed Abstract: Archaea possess a basal transcriptional apparatus that resembles that of eukaryotes. Here we report the 2.1-A crystal structure of the archaeal transcription factor complex formed by the TATA-box-binding protein (TBP), the transcription factor IIB homolog, and a DNA target, all from the hyperthermophile Pyrococcus woesei. The overall fold of these two basal transcription factors is essentially the same as that of their eukaryotic counterparts. However, in comparison with the eukaryotic complexes, the archaeal TBP-DNA interface is more symmetrical, and in this structure the orientation of the preinitiation complex assembly on the promoter is inverted with respect to that seen in all crystal structures of comparable eukaryotic systems. This study of the structural details of an archaeal transcription factor complex presents the opportunity to examine the evolution of the basal eukaryotic transcriptional apparatus from a stereochemical viewpoint and to extend our understanding of the physical biochemistry of transcriptional initiation.

PubMed: 9177165
DOI: 10.1073/pnas.94.12.6042

Experimental method

X-RAY DIFFRACTION (2.1 Å)