1Y1V
Refined RNA Polymerase II-TFIIS complex
Summary for 1Y1V
Entry DOI | 10.2210/pdb1y1v/pdb |
Related | 1PQV |
Descriptor | DNA-directed RNA polymerase II largest subunit, DNA-directed RNA polymerases I/II/III subunit 10, DNA-directed RNA polymerase II 13.6 kDa polypeptide, ... (15 entities in total) |
Functional Keywords | rna polymerase ii, tfiis, transcription, elongation, transferase-transcription complex, transferase/transcription |
Biological source | Saccharomyces cerevisiae (baker's yeast) More |
Total number of polymer chains | 13 |
Total formula weight | 535043.15 |
Authors | Kettenberger, H.,Armache, K.-J.,Cramer, P. (deposition date: 2004-11-19, release date: 2004-12-28, Last modification date: 2024-03-13) |
Primary citation | Kettenberger, H.,Armache, K.J.,Cramer, P. Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS. Mol.Cell, 16:955-965, 2004 Cited by PubMed Abstract: The crystal structure of the complete 12 subunit RNA polymerase (pol) II bound to a transcription bubble and product RNA reveals incoming template and nontemplate DNA, a seven base pair DNA/RNA hybrid, and three nucleotides each of separating DNA and RNA. The complex adopts the posttranslocation state and accommodates a cocrystallized nucleoside triphosphate (NTP) substrate. The NTP binds in the active site pore at a position to interact with a DNA template base. Residues surrounding the NTP are conserved in all cellular RNA polymerases, suggesting a universal mechanism of NTP selection and incorporation. DNA-DNA and DNA-RNA strand separation may be explained by pol II-induced duplex distortions. Four protein loops partition the active center cleft, contribute to embedding the hybrid, prevent strand reassociation, and create an RNA exit tunnel. Binding of the elongation factor TFIIS realigns RNA in the active center, possibly converting the elongation complex to an alternative state less prone to stalling. PubMed: 15610738DOI: 10.1016/j.molcel.2004.11.040 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.8 Å) |
Structure validation
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