Structural basis of transcription: RNA Polymerase II substrate binding and metal coordination at 3.0 A using a free-electron laser.

ABSTRACT: Catalysis and translocation of multi-subunit DNA-directed RNA polymerases underlie all cellular mRNA synthesis. RNA polymerase II (Pol II) synthesizes eukaryotic pre-mRNAs from a DNA template strand buried in its active site. Structural details of catalysis at near atomic resolution and precise arrangement of key active site components have been elusive. Here we present the free electron laser (FEL) structure of a matched ATP-bound Pol II, revealing the full active site interaction network at the highest resolution to date, including the trigger loop (TL) in the closed conformation, bonafide occupancy of both site A and B Mg²⁺, and a putative third (site C) Mg²⁺ analogous to that described for some DNA polymerases but not observed previously for cellular RNA polymeras

SUBMITTER: Lin G 

PROVIDER: S-EPMC10543002 | biostudies-literature | 2023 Sep

REPOSITORIES: biostudies-literature