1IW7

Crystal structure of the RNA polymerase holoenzyme from Thermus thermophilus at 2.6A resolution

Summary for 1IW7

• Entry DOI: 10.2210/pdb1iw7/pdb
• Descriptor: RNA polymerase alpha subunit, RNA polymerase beta subunit, RNA polymerase omega subunit, ... (8 entities in total)
• Functional Keywords: rna polymerase holoenzyme, riken structural genomics/proteomics initiative, rsgi, structural genomics, transferase
• Biological source: Thermus thermophilus; More
• Total number of polymer chains: 12
• Total formula weight: 865887.70

Authors

RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2002-04-22, release date: 2002-06-26, Last modification date: 2023-10-25)

Primary citation

Vassylyev, D.G.,Sekine, S.,Laptenko, O.,Lee, J.,Vassylyeva, M.N.,Borukhov, S.,Yokoyama, S.
Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 A resolution
NATURE, 417:712-719, 2002

PubMed Abstract: In bacteria, the binding of a single protein, the initiation factor sigma, to a multi-subunit RNA polymerase core enzyme results in the formation of a holoenzyme, the active form of RNA polymerase essential for transcription initiation. Here we report the crystal structure of a bacterial RNA polymerase holoenzyme from Thermus thermophilus at 2.6 A resolution. In the structure, two amino-terminal domains of the sigma subunit form a V-shaped structure near the opening of the upstream DNA-binding channel of the active site cleft. The carboxy-terminal domain of sigma is near the outlet of the RNA-exit channel, about 57 A from the N-terminal domains. The extended linker domain forms a hairpin protruding into the active site cleft, then stretching through the RNA-exit channel to connect the N- and C-terminal domains. The holoenzyme structure provides insight into the structural organization of transcription intermediate complexes and into the mechanism of transcription initiation.

PubMed: 12000971
DOI: 10.1038/nature752

Experimental method

X-RAY DIFFRACTION (2.6 Å)