8a40 | pdb_00008a40

Structure of mammalian Pol II-TFIIS elongation complex

spinqualitylabelsall models 8a40, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8a40 is a 10 chain structure with sequence from Homo sapiens, Sus scrofa and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3Å Ligands: MG, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A7M4DUC2_PIG DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[RuleBase:RU004279] Publication Abstract from PubMed During gene transcription, RNA polymerase II (RNA Pol II) passes nucleosomes with the help of various elongation factors. Here, we show that RNA Pol II achieves efficient nucleosome passage when the human elongation factors DSIF, PAF1 complex (PAF), RTF1, SPT6, and TFIIS are present. The cryo-EM structure of an intermediate of the nucleosome passage shows a partially unraveled hexasome that lacks the proximal H2A-H2B dimer and interacts with the RNA Pol II jaw, DSIF, and the CTR9trestle helix. RNA Pol II adopts a backtracked state with the RNA 3' end dislodged from the active site and bound in the RNA Pol II pore. Additional structures and biochemical data show that human TFIIS enters the RNA Pol II pore and stimulates the cleavage of the backtracked RNA and nucleosome passage. Structure of a backtracked hexasomal intermediate of nucleosome transcription.,Farnung L, Ochmann M, Garg G, Vos SM, Cramer P Mol Cell. 2022 Sep 1;82(17):3126-3134.e7. doi: 10.1016/j.molcel.2022.06.027. Epub , 2022 Jul 19. PMID:35858621 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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