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

Research output: Contribution to journalArticlepeer-review

187 Scopus citations


The X-ray crystal structure of Thermus aquaticus core RNA polymerase reveals a "crab claw"-shaped molecule with a 27 Å 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.

Original languageEnglish (US)
Pages (from-to)811-824
Number of pages14
Issue number6
StatePublished - Sep 17 1999

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)


Dive into the research topics of 'Crystal structure of thermus aquaticus core RNA polymerase at 3.3 å resolution'. Together they form a unique fingerprint.

Cite this