NDLI: Conformational flexibility of bacterial RNA polymerase.

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Conformational flexibility of bacterial RNA polymerase.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Opalka, Natacha Polyakov, Andrey Darst, Seth A. Chacon, Pablo Wriggers, Willy Zhang, Gongyi Richter, Catherine
Description	Author Affiliation: Darst SA ( Laboratory of Molecular Biophysics, The Rockefeller University, New York, NY 10021, USA. darst@rockefeller.edu);
Abstract	The structure of Escherichia coli core RNA polymerase (RNAP) was determined by cryo-electron microscopy and image processing of helical crystals to a nominal resolution of 15 A. Because of the high sequence conservation between the core RNAP subunits, we were able to interpret the E. coli structure in relation to the high-resolution x-ray structure of Thermus aquaticus core RNAP. A very large conformational change of the T. aquaticus RNAP x-ray structure, corresponding to opening of the main DNA/RNA channel by nearly 25 A, was required to fit the E. coli map. This finding reveals, at least partially, the range of conformational flexibility of the RNAP, which is likely to have functional implications for the initiation of transcription, where the DNA template must be loaded into the channel.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	7
Volume Number	99
Language	English
Publisher	National Academy of Sciences
Publisher Date	2002-04-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	DNA-Directed RNA Polymerases Chemistry Escherichia Coli Enzymology Crystallization Microscopy, Electron Protein Conformation Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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