Structural basis of transcription: alpha-amanitin-RNA polymerase II cocrystal at 2.8 A resolution.
The structure of RNA polymerase II in a complex with the inhibitor alpha-amanitin has been determined by x-ray crystallography. The structure of the complex indicates the likely basis of inhibition and gives unexpected insight into the transcription mechanism.
Bushnell
David A
DA
Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305-5126, USA.
Cramer
Patrick
P
Kornberg
Roger D
RD
D000546:Amanitins / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D018360:Crystallography, X-Ray / Q000379:methods; D006860:Hydrogen Bonding; D008958:Models, Molecular; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012319:RNA Polymerase II / Q000737:chemistry*; D014158:Transcription, Genetic
D000546:Amanitins; D012319:RNA Polymerase II