Summary information and primary citation

PDB-id
8oew; SNAP-derived features in text and JSON formats; DNAproDB
Class
transcription
Method
cryo-EM (2.8 Å)
Summary
Structure of the mammalian pol ii-elongin complex, lacking the eloa latch (composite structure, structure 2)
Reference
Chen Y, Kokic G, Dienemann C, Dybkov O, Urlaub H, Cramer P (2023): "Structure of the transcribing RNA polymerase II-Elongin complex." Nat.Struct.Mol.Biol., 30, 1925-1935. doi: 10.1038/s41594-023-01138-w.
Abstract
Elongin is a heterotrimeric elongation factor for RNA polymerase (Pol) II transcription that is conserved among metazoa. Here, we report three cryo-EM structures of human Elongin bound to transcribing Pol II. The structures show that Elongin subunit ELOA binds the RPB2 side of Pol II and anchors the ELOB-ELOC subunit heterodimer. ELOA contains a 'latch' that binds between the end of the Pol II bridge helix and funnel helices, thereby inducing a conformational change near the polymerase active center. The latch is required for the elongation-stimulatory activity of Elongin, but not for Pol II binding, indicating that Elongin functions by allosterically regulating the conformational mobility of the polymerase active center. Elongin binding to Pol II is incompatible with association of the super elongation complex, PAF1 complex and RTF1, which also contain an elongation-stimulatory latch element.

Cartoon-block schematics in six views (download the tarball)

PyMOL session file Download PDB file View in 3Dmol.js