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1Y1V

Refined RNA Polymerase II-TFIIS complex

Summary for 1Y1V
Entry DOI10.2210/pdb1y1v/pdb
Related1PQV
DescriptorDNA-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 Keywordsrna polymerase ii, tfiis, transcription, elongation, transferase-transcription complex, transferase/transcription
Biological sourceSaccharomyces cerevisiae (baker's yeast)
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Total number of polymer chains13
Total formula weight535043.15
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 citationKettenberger, 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: 15610738
DOI: 10.1016/j.molcel.2004.11.040
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.8 Å)
Structure validation

226707

数据于2024-10-30公开中

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