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Article

Conformational coupling, bridge helix dynamics and active site dehydration in catalysis by RNA polymerase.

Biochimica et biophysica acta - 1 Aug 2010

Seibold Steve A, Singh Badri Nath, Zhang Chunfen, Kireeva Maria, Domecq Céline, Bouchard Annie, Nazione Anthony M, Feig Michael, Cukier Robert I, Coulombe Benoit, Kashlev Mikhail, Hampsey Michael, Burton Zachary F

Abstract excerpt

Molecular dynamics simulation of Thermus thermophilus (Tt) RNA polymerase (RNAP) in a catalytic conformation demonstrates that the active site dNMP-NTP base pair must be substantially dehydrated to support full active site closing and optimum conditions for phosphodiester bond synthesis. In silico mutant beta R428A RNAP, which was designed based on substitutions at the homologous position (Rpb2 R512) of...

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Identifiers

PMID: 20478425
DOI: 10.1016/j.bbagrm.2010.05.002
PMCID: PMC2922424

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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