Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8OF0

Structure of the mammalian Pol II-SPT6-Elongin complex, Structure 1

Summary for 8OF0
Entry DOI10.2210/pdb8of0/pdb
EMDB information16836 16840
DescriptorDNA-directed RNA polymerase II subunit RPB1, DNA-directed RNA polymerases I, II, and III subunit RPABC5, DNA-directed RNA polymerase II subunit RPB11-a, ... (21 entities in total)
Functional Keywordstranscription elongation, elongin, rna polymerase ii, transcription
Biological sourceHomo sapiens (human)
More
Total number of polymer chains19
Total formula weight890993.47
Authors
Chen, Y.,Kokic, G.,Dienemann, C.,Dybkov, O.,Urlaub, H.,Cramer, P. (deposition date: 2023-03-13, release date: 2023-10-18, Last modification date: 2023-12-27)
Primary citationChen, Y.,Kokic, G.,Dienemann, C.,Dybkov, O.,Urlaub, H.,Cramer, P.
Structure of the transcribing RNA polymerase II-Elongin complex.
Nat.Struct.Mol.Biol., 30:1925-1935, 2023
Cited by
PubMed 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.
PubMed: 37932450
DOI: 10.1038/s41594-023-01138-w
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.05 Å)
Structure validation

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon