Crystal Structure of Thermus aquaticus Core RNA Polymerase at 3.3 Å Resolution
Gongyi Zhang,Elizabeth A. Campbell,Leonid Minakhin,Catherine Richter,Konstantin Severinov,Seth A. Darst +5 more
TLDR
The X-ray crystal structure of Thermus aquaticus core RNA polymerase reveals a "crab claw"-shaped molecule with a 27 A wide internal channel that 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+.About:
This article is published in Cell.The article was published on 1999-09-17 and is currently open access. It has received 814 citations till now. The article focuses on the topics: Thermus aquaticus & RNA polymerase.read more
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Structural Mechanism for Rifampicin Inhibition of Bacterial RNA Polymerase
Elizabeth A. Campbell,Nataliya Korzheva,Arkady Mustaev,Katsuhiko S. Murakami,Satish K. Nair,Alex Goldfarb,Seth A. Darst +6 more
TL;DR: The crystal structure of Thermus aquaticus core RNAP complexed with Rif explains the effects of Rif on RNAP function and indicates that the inhibitor acts by directly blocking the path of the elongating RNA when the transcript becomes 2 to 3 nt in length.
Journal ArticleDOI
Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution.
TL;DR: Structures of a 10-subunit yeast RNA polymerase II derived from two crystal forms at 2.8 and 3.1 angstrom resolution provide evidence for RNA exit in the vicinity of the carboxyl-terminal repeat domain, coupling synthesis to RNA processing by enzymes bound to this domain.
Journal ArticleDOI
The protein-protein interaction map of Helicobacter pylori.
Jean-Christophe Rain,Luc Selig,Hilde De Reuse,Véronique Battaglia,Céline Reverdy,Stéphane Simon,Gerlinde Lenzen,Fabien Petel,Jérôme Wojcik,Vincent Schächter,Y. Chemama,Agnès Labigne,Pierre Legrain +12 more
TL;DR: A large-scale protein–protein interaction map of the human gastric pathogen Helicobacter pylori is built and the assignment of unannotated proteins to biological pathways is permitted.
Journal ArticleDOI
The regulation of bacterial transcription initiation
TL;DR: Bacteria use their genetic material with great effectiveness to make the right products in the correct amounts at the appropriate time, but for reasons of economy, the key step to regulate is the initiation of RNA-transcript formation.
Journal ArticleDOI
Structural Basis of Transcription: An RNA Polymerase II Elongation Complex at 3.3 Å Resolution
TL;DR: The crystal structure of RNA polymerase II in the act of transcription was determined at 3.3 Å resolution and protein–nucleic acid contacts help explain DNA and RNA strand contacts, the specificity of RNA synthesis, “abortive cycling” during transcription initiation, and RNA and DNA translocation during transcription elongation.
References
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