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

6TED

Structure of complete, activated transcription complex Pol II-DSIF-PAF-SPT6 uncovers allosteric elongation activation by RTF1

Summary for 6TED
Entry DOI10.2210/pdb6ted/pdb
EMDB information10480
DescriptorDNA-directed RNA polymerase subunit, Uncharacterized protein, Transcription elongation factor SPT6, ... (26 entities in total)
Functional Keywordspolymerase, elongation complex, rna, dna, transcription
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains24
Total formula weight1351868.46
Authors
Vos, S.M.,Farnung, L.,Cramer, P. (deposition date: 2019-11-11, release date: 2020-07-22, Last modification date: 2024-10-23)
Primary citationVos, S.M.,Farnung, L.,Linden, A.,Urlaub, H.,Cramer, P.
Structure of complete Pol II-DSIF-PAF-SPT6 transcription complex reveals RTF1 allosteric activation.
Nat.Struct.Mol.Biol., 27:668-677, 2020
Cited by
PubMed Abstract: Transcription by RNA polymerase II (Pol II) is carried out by an elongation complex. We previously reported an activated porcine Pol II elongation complex, EC*, encompassing the human elongation factors DSIF, PAF1 complex (PAF) and SPT6. Here we report the cryo-EM structure of the complete EC* that contains RTF1, a dissociable PAF subunit critical for chromatin transcription. The RTF1 Plus3 domain associates with Pol II subunit RPB12 and the phosphorylated C-terminal region of DSIF subunit SPT5. RTF1 also forms four α-helices that extend from the Plus3 domain along the Pol II protrusion and RPB10 to the polymerase funnel. The C-terminal 'fastener' helix retains PAF and is followed by a 'latch' that reaches the end of the bridge helix, a flexible element of the Pol II active site. RTF1 strongly stimulates Pol II elongation, and this requires the latch, possibly suggesting that RTF1 activates transcription allosterically by influencing Pol II translocation.
PubMed: 32541898
DOI: 10.1038/s41594-020-0437-1
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.1 Å)
Structure validation

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon