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Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 angstrom resolution
Author(s): Zhang GY, Campbell EA, Minakhin L, Richter C, Severinov K, Darst SA
Source: CELL    Volume: 98    Issue: 6    Pages: 811-824    Published: SEP 17 1999  
Times Cited: 416     References: 61     
Abstract: The X-ray crystal structure of Thermus aquaticus core RNA polymerase reveals a "crab claw"-shaped molecule with a 27 Angstrom wide internal channel. Located on the back wall of the channel is a Mg2+ ion required for catalytic activity, which is chelated by an absolutely conserved motif from all bacterial and eukaryotic cellular RNA polymerases. The structure places key functional sites, defined by mutational and cross-linking analysis, on the inner walls of the channel in close proximity to the active center Mg2+. Further out from the catalytic center, structural features are found that may be involved in maintaining the melted transcription bubble, clamping onto the RNA product and/or DNA template to assure processivity, and delivering nucleotide substrates to the active center.
Document Type: Article
Language: English
Reprint Address: Darst, SA (reprint author), Rockefeller Univ, 1230 York Ave, New York, NY 10021 USA
Addresses:
1. Rockefeller Univ, New York, NY 10021 USA
2. Rutgers State Univ, Waksman Inst, Piscataway, NJ 08854 USA
3. Rutgers State Univ, Dept Genet, Piscataway, NJ 08854 USA
Publisher: CELL PRESS, 1050 MASSACHUSETTES AVE, CIRCULATION DEPT, CAMBRIDGE, MA 02138 USA
Subject Category: Biochemistry & Molecular Biology; Cell Biology
IDS Number: 237WH
ISSN: 0092-8674
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