5oik

Structure of an RNA polymerase II-DSIF transcription elongation complexStructure of an RNA polymerase II-DSIF transcription elongation complex

5oik, resolution 3.70Å Show:Asymmetric Unit Biological Assembly Structural highlights 5oik is a 10 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.7Å Ligands: Experimental data: Check Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G3MZY8_BOVIN 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 transcription, RNA polymerase II (Pol II) associates with the conserved elongation factor DSIF. DSIF renders the elongation complex stable and functions during Pol II pausing and RNA processing. We combined cryo-EM and X-ray crystallography to determine the structure of the mammalian Pol II-DSIF elongation complex at a nominal resolution of 3.4 A. Human DSIF has a modular structure with two domains forming a DNA clamp, two domains forming an RNA clamp, and one domain buttressing the RNA clamp. The clamps maintain the transcription bubble, position upstream DNA, and retain the RNA transcript in the exit tunnel. The mobile C-terminal region of DSIF is located near exiting RNA, where it can recruit factors for RNA processing. The structure provides insight into the roles of DSIF during mRNA synthesis. Structure of a transcribing RNA polymerase II-DSIF complex reveals a multidentate DNA-RNA clamp.,Bernecky C, Plitzko JM, Cramer P Nat Struct Mol Biol. 2017 Sep 11. doi: 10.1038/nsmb.3465. PMID:28892040 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Elongation factor 3D structures RNA polymerase 3D structures