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3GTP

Backtracked RNA polymerase II complex with 24mer RNA

Summary for 3GTP
Entry DOI10.2210/pdb3gtp/pdb
Related3GTG 3GTJ 3GTK 3GTL 3GTM 3GTO 3GTQ
DescriptorDNA-directed RNA polymerase II subunit RPB1, DNA-directed RNA polymerases I, II, and III subunit RPABC4, RNA (5'-R(*AP*UP*CP*GP*AP*GP*AP*GP*GP*AP*UP*GP*CP*AP*GP*AP*CP*GP*UP*UP*UP*UP*UP*U)-3'), ... (15 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, transferase-dna-rna hybrid complex, transferase/dna-rna hybrid
Biological sourceSaccharomyces cerevisiae (yeast)
More
Cellular locationNucleus: P04050 P08518 P16370 P20434 P20436 P38902
Nucleus, nucleolus : P40422 P27999 P22139
Cytoplasm : P20435
Total number of polymer chains13
Total formula weight490706.45
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: 2024-10-30)
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 (3.9 Å)
Structure validation

226707

건을2024-10-30부터공개중

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