2O5I

Crystal structure of the T. thermophilus RNA polymerase elongation complex

Summary for 2O5I

• Entry DOI: 10.2210/pdb2o5i/pdb
• Related: 2O5J
• Descriptor: 5'-D(P*CP*CP*CP*TP*GP*TP*CP*TP*GP*GP*CP*GP*TP*TP*CP*GP*CP*GP*CP*GP*CP*CP*G)-3', 5'-R(P*GP*AP*GP*UP*CP*UP*GP*CP*GP*GP*CP*GP*CP*GP*CP*G)-3', 5'-D(*AP*AP*CP*GP*CP*CP*AP*GP*AP*CP*AP*GP*GP*G)-3', ... (10 entities in total)
• Functional Keywords: rna polymerase, elongation complex, template dna, non-template dna, rna transcript, transferase-dna-rna hybrid complex, transferase/dna-rna hybrid
• Biological source: Thermus thermophilus; More
• Total number of polymer chains: 16
• Total formula weight: 789488.27

Authors

Vassylyev, D.G.,Tahirov, T.H.,Vassylyeva, M.N. (deposition date: 2006-12-06, release date: 2007-07-03, Last modification date: 2023-08-30)

Primary citation

Vassylyev, D.G.,Vassylyeva, M.N.,Perederina, A.,Tahirov, T.H.,Artsimovitch, I.
Structural basis for transcription elongation by bacterial RNA polymerase.
Nature, 448:157-162, 2007

PubMed Abstract: The RNA polymerase elongation complex (EC) is both highly stable and processive, rapidly extending RNA chains for thousands of nucleotides. Understanding the mechanisms of elongation and its regulation requires detailed information about the structural organization of the EC. Here we report the 2.5-A resolution structure of the Thermus thermophilus EC; the structure reveals the post-translocated intermediate with the DNA template in the active site available for pairing with the substrate. DNA strand separation occurs one position downstream of the active site, implying that only one substrate at a time can specifically bind to the EC. The upstream edge of the RNA/DNA hybrid stacks on the beta'-subunit 'lid' loop, whereas the first displaced RNA base is trapped within a protein pocket, suggesting a mechanism for RNA displacement. The RNA is threaded through the RNA exit channel, where it adopts a conformation mimicking that of a single strand within a double helix, providing insight into a mechanism for hairpin-dependent pausing and termination.

PubMed: 17581590
DOI: 10.1038/nature05932

Experimental method

X-RAY DIFFRACTION (2.5 Å)