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Structural basis of transcription: An RNA polymerase II elongation complex at 3.3 angstrom resolution
Author(s): Gnatt AL, Cramer P, Fu JH, Bushnell DA, Kornberg RD
Source: SCIENCE    Volume: 292    Issue: 5523    Pages: 1876-1882    Published: JUN 8 2001  
Times Cited: 401     References: 40     
Abstract: The crystal structure of RNA polymerase II in the act of transcription was determined at 3.3 Angstrom resolution. Duplex DNA is seen entering the main cleft of the enzyme and unwinding before the active site. Nine base pairs of DNA-RNA hybrid extend from the active center at nearly right angles to the entering DNA, with the 3' end of the RNA in the nucleotide addition site. The 3' end is positioned above a pore, through which nucleotides may enter and through which RNA may be extruded during back-tracking. The 5'-most residue of the RNA is close to the point of entry to an exit groove. Changes in protein structure between the transcribing complex and free enzyme include closure of a clamp over the DNA and RNA and ordering of a series of "switches" at the base of the clamp to create a binding site complementary to the DNA-RNA hybrid. Protein-nucleic acid contacts help explain DNA and RNA strand separation, the specificity of RNA synthesis, "abortive cycling" during transcription initiation, and RNA and DNA translocation during transcription elongation.
Document Type: Article
Language: English
Reprint Address: Kornberg, RD (reprint author), Stanford Univ, Sch Med, Dept Biol Struct, Stanford, CA 94305 USA
Addresses:
1. Stanford Univ, Sch Med, Dept Biol Struct, Stanford, CA 94305 USA
Publisher: AMER ASSOC ADVANCEMENT SCIENCE, 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005 USA
Subject Category: Multidisciplinary Sciences
IDS Number: 440WY
ISSN: 0036-8075
DOI: 10.1126/science.1059495
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