Active-site dynamics in RNA polymerases
- PMID: 15016367
- DOI: 10.1016/s0092-8674(04)00121-7
Active-site dynamics in RNA polymerases
Abstract
New crystal structures of transcription complexes formed by bacteriophage T7 RNA polymerase reveal a nucleotide-addition cycle driven by active-site conformational changes similar to those observed in DNA polymerases, and suggest provocative hypotheses for the more complex multisubunit RNA polymerases of free-living organisms.
Comment on
-
Structural basis for substrate selection by t7 RNA polymerase.Cell. 2004 Feb 6;116(3):381-91. doi: 10.1016/s0092-8674(04)00059-5. Cell. 2004. PMID: 15016373
-
The structural mechanism of translocation and helicase activity in T7 RNA polymerase.Cell. 2004 Feb 6;116(3):393-404. doi: 10.1016/s0092-8674(04)00120-5. Cell. 2004. PMID: 15016374
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
