1H38

Structure of a T7 RNA polymerase elongation complex at 2.9A resolution

Summary for 1H38

• Entry DOI: 10.2210/pdb1h38/pdb
• Related: 1ARO 1CEZ 1QLN 4RNP
• Descriptor: DNA-DIRECTED RNA POLYMERASE, 5'-D(*GP*GP*GP*AP*AP*TP*CP*GP*AP*CP *AP*TP*CP*GP*CP*CP*GP*C)-3', 5'-R(*AP*AP*CP*UP*GP*CP*GP*GP*CP*GP *AP*U)-3', ... (5 entities in total)
• Functional Keywords: transferase, rna polymerase, t7 rna polymerase, elongation complex, protein/dna/rna, riken structural genomics/proteomics initiative, rsgi, structural genomics
• Biological source: BACTERIOPHAGE T7; More
• Total number of polymer chains: 16
• Total formula weight: 445432.54

Authors

Tahirov, T.H.,Temyakov, D.,Anikin, M.,Patlan, V.,McAllister, W.T.,Vassylyev, D.G.,Yokoyama, S. (deposition date: 2002-08-24, release date: 2002-11-20, Last modification date: 2023-12-13)

Primary citation

Tahirov, T.H.,Temiakov, D.,Anikin, M.,Patlan, V.,Mcallister, W.T.,Vassylyev, D.G.,Yokoyama, S.
Structure of a T7 RNA Polymerase Elongation Complex at 2.9 A Resolution
Nature, 420:43-, 2002

PubMed Abstract: The single-subunit bacteriophage T7 RNA polymerase carries out the transcription cycle in an identical manner to that of bacterial and eukaryotic multisubunit enzymes. Here we report the crystal structure of a T7 RNA polymerase elongation complex, which shows that incorporation of an 8-base-pair RNA-DNA hybrid into the active site of the enzyme induces a marked rearrangement of the amino-terminal domain. This rearrangement involves alternative folding of about 130 residues and a marked reorientation (about 130 degrees rotation) of a stable core subdomain, resulting in a structure that provides elements required for stable transcription elongation. A wide opening on the enzyme surface that is probably an RNA exit pathway is formed, and the RNA-DNA hybrid is completely buried in a newly formed, deep protein cavity. Binding of 10 base pairs of downstream DNA is stabilized mostly by long-distance electrostatic interactions. The structure implies plausible mechanisms for the various phases of the transcription cycle, and reveals important structural similarities with the multisubunit RNA polymerases.

PubMed: 12422209
DOI: 10.1038/NATURE01129

Experimental method

X-RAY DIFFRACTION (2.9 Å)