3I4N
8-oxoguanine containing RNA polymerase II elongation complex E
Summary for 3I4N
Entry DOI | 10.2210/pdb3i4n/pdb |
Related | 3I4M |
Descriptor | DNA-directed RNA polymerase II subunit RPB1, DNA-directed RNA polymerases I, II, and III subunit RPABC5, DNA-directed RNA polymerase II subunit RPB11, ... (17 entities in total) |
Functional Keywords | rna polymerase ii, metal-binding, transcription bubble, elongation complex, transcription, 8-oxoguanine, dna damage, oxidative damage, dna-binding, dna-directed rna polymerase, isopeptide bond, magnesium, nucleotidyltransferase, nucleus, phosphoprotein, transferase, zinc-finger, dna repair, mrna processing, transferase-dna-rna hybrid complex, transferase/dna-rna hybrid |
Biological source | Saccharomyces cerevisiae (baker's yeast) More |
Cellular location | Nucleus: P04050 P38902 P08518 P16370 P20433 P20434 P34087 P20436 P27999 Nucleus, nucleolus: P22139 P40422 Cytoplasm: P20435 |
Total number of polymer chains | 15 |
Total formula weight | 532306.12 |
Authors | Damsma, G.E.,Cramer, P. (deposition date: 2009-07-02, release date: 2009-09-08, Last modification date: 2024-10-30) |
Primary citation | Damsma, G.E.,Cramer, P. Molecular basis of transcriptional mutagenesis at 8-oxoguanine J.Biol.Chem., 284:31658-31663, 2009 Cited by PubMed Abstract: Structure-function analysis has revealed the mechanism of yeast RNA polymerase II transcription at 8-oxoguanine (8-oxoG), the major DNA lesion resulting from oxidative stress. When polymerase II encounters 8-oxoG in the DNA template strand, it can misincorporate adenine, which forms a Hoogsteen bp with 8-oxoG at the active center. This requires rotation of the 8-oxoG base from the standard anti- to an uncommon syn-conformation, which likely occurs during 8-oxoG loading into the active site. The misincorporated adenine escapes intrinsic proofreading, resulting in transcriptional mutagenesis that is observed directly by mass spectrometric RNA analysis. PubMed: 19758983DOI: 10.1074/jbc.M109.022764 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.9 Å) |
Structure validation
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