1L9Z

Thermus aquaticus RNA Polymerase Holoenzyme/Fork-Junction Promoter DNA Complex at 6.5 A Resolution

Summary for 1L9Z

• Entry DOI: 10.2210/pdb1l9z/pdb
• Descriptor: nontemplate DNA strand, template DNA strand, RNA POLYMERASE, ALPHA SUBUNIT, ... (9 entities in total)
• Functional Keywords: helix-turn-helix, coiled-coil, transcription-dna complex, transcription/dna
• Biological source: Thermus aquaticus; More
• Total number of polymer chains: 8
• Total formula weight: 447339.55

Authors

Murakami, K.S.,Masuda, S.,Campbell, E.A.,Muzzin, O.,Darst, S.A. (deposition date: 2002-03-27, release date: 2002-05-31, Last modification date: 2024-02-14)

Primary citation

Murakami, K.S.,Masuda, S.,Campbell, E.A.,Muzzin, O.,Darst, S.A.
Structural basis of transcription initiation: an RNA polymerase holoenzyme-DNA complex.
Science, 296:1285-1290, 2002

PubMed Abstract: The crystal structure of Thermus aquaticus RNA polymerase holoenzyme (alpha2betabeta'omegasigmaA) complexed with a fork-junction promoter DNA fragment has been determined by fitting high-resolution x-ray structures of individual components into a 6.5-angstrom resolution map. The DNA lies across one face of the holoenzyme, completely outside the RNA polymerase active site channel. All sequence-specific contacts with core promoter elements are mediated by the sigma subunit. A universally conserved tryptophan is ideally positioned to stack on the exposed face of the base pair at the upstream edge of the transcription bubble. Universally conserved basic residues of the sigma subunit provide critical contacts with the DNA phosphate backbone and play a role in directing the melted DNA template strand into the RNA polymerase active site. The structure explains how holoenzyme recognizes promoters containing variably spaced -10 and -35 elements and provides the basis for models of the closed and open promoter complexes.

PubMed: 12016307
DOI: 10.1126/science.1069595

Experimental method

X-RAY DIFFRACTION (6.5 Å)