5FMF
the P-lobe of RNA polymerase II pre-initiation complex
Summary for 5FMF
Entry DOI | 10.2210/pdb5fmf/pdb |
EMDB information | 3114 |
Descriptor | DNA REPAIR HELICASE RAD25, SSL2, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC3, RPB8, DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB9, ... (29 entities in total) |
Functional Keywords | transcription, pre-initiation complex, rna polymerase, tfiie, tfiih, tfiib, tbp, tfiif, protein |
Biological source | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) More |
Cellular location | Nucleus: P04050 P38902 P29055 P13393 P36100 P36145 P08518 P41896 Q02939 Q3E7C1 P06839 Q00578 P07273 P16370 P20434 P34087 P20436 Nucleus, nucleolus : P22139 P40422 P27999 Cytoplasm : P32774 P20435 |
Total number of polymer chains | 27 |
Total formula weight | 873735.25 |
Authors | Murakami, K.,Tsai, K.,Kalisman, N.,Bushnell, D.A.,Asturias, F.J.,Kornberg, R.D. (deposition date: 2015-11-03, release date: 2015-11-25, Last modification date: 2024-11-20) |
Primary citation | Murakami, K.,Tsai, K.,Kalisman, N.,Bushnell, D.A.,Asturias, F.J.,Kornberg, R.D. Structure of an RNA Polymerase II Pre-Initiation Complex Proc.Natl.Acad.Sci.USA, 112:13543-, 2015 Cited by PubMed Abstract: The structure of a 33-protein, 1.5-MDa RNA polymerase II preinitiation complex (PIC) was determined by cryo-EM and image processing at a resolution of 6-11 Å. Atomic structures of over 50% of the mass were fitted into the electron density map in a manner consistent with protein-protein cross-links previously identified by mass spectrometry. The resulting model of the PIC confirmed the main conclusions from previous cryo-EM at lower resolution, including the association of promoter DNA only with general transcription factors and not with the polymerase. Electron density due to DNA was identifiable by the grooves of the double helix and exhibited sharp bends at points downstream of the TATA box, with an important consequence: The DNA at the downstream end coincides with the DNA in a transcribing polymerase. The structure of the PIC is therefore conducive to promoter melting, start-site scanning, and the initiation of transcription. PubMed: 26483468DOI: 10.1073/PNAS.1518255112 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (6 Å) |
Structure validation
Download full validation report
