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3GTM

Co-complex of Backtracked RNA polymerase II with TFIIS

Summary for 3GTM
Entry DOI10.2210/pdb3gtm/pdb
Related3GTG 3GTJ 3GTK 3GTL 3GTO 3GTP 3GTQ
DescriptorDNA-directed RNA polymerase II subunit RPB1, DNA-directed RNA polymerases I, II, and III subunit RPABC4, Transcription elongation factor S-II, ... (16 entities in total)
Functional Keywordstranscription, transferase, dna-rna hybrid, backtrack, dna-directed rna polymerase, dna binding, isopeptide bond, magnesium, metal binding, nucleotidyltransferase, nucleus, phosphoprotein, ubl conjugation, zinc, zinc-finger, polymorphism, cytoplasm, dna damage, dna repair, transcription regulation, transferase-dna-rna hybrid complex, transferase/dna-rna hybrid
Biological sourceSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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Total number of polymer chains14
Total formula weight507013.29
Authors
Wang, D.,Bushnell, D.A.,Huang, X.,Westover, K.D.,Levitt, M.,Kornberg, R.D. (deposition date: 2009-03-27, release date: 2009-06-09, Last modification date: 2024-10-09)
Primary citationWang, D.,Bushnell, D.A.,Huang, X.,Westover, K.D.,Levitt, M.,Kornberg, R.D.
Structural basis of transcription: backtracked RNA polymerase II at 3.4 angstrom resolution.
Science, 324:1203-1206, 2009
Cited by
PubMed Abstract: Transcribing RNA polymerases oscillate between three stable states, two of which, pre- and posttranslocated, were previously subjected to x-ray crystal structure determination. We report here the crystal structure of RNA polymerase II in the third state, the reverse translocated, or "backtracked" state. The defining feature of the backtracked structure is a binding site for the first backtracked nucleotide. This binding site is occupied in case of nucleotide misincorporation in the RNA or damage to the DNA, and is termed the "P" site because it supports proofreading. The predominant mechanism of proofreading is the excision of a dinucleotide in the presence of the elongation factor SII (TFIIS). Structure determination of a cocrystal with TFIIS reveals a rearrangement whereby cleavage of the RNA may take place.
PubMed: 19478184
DOI: 10.1126/science.1168729
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.8 Å)
Structure validation

226707

數據於2024-10-30公開中

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