2JA8
CPD lesion containing RNA Polymerase II elongation complex D
2JA8 の概要
エントリーDOI | 10.2210/pdb2ja8/pdb |
関連するPDBエントリー | 1A1D 1DZF 1I3Q 1I50 1I6H 1K83 1NIK 1NT9 1PQV 1R5U 1R9S 1R9T 1SFO 1TWA 1TWC 1TWF 1TWG 1TWH 1WCM 1Y14 1Y1V 1Y1W 1Y1Y 1Y77 2B63 2B8K 2JA5 2JA6 2JA7 |
分子名称 | 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, ... (17 entities in total) |
機能のキーワード | dna-directed rna polymerase, lesion recognition, transferase/dna/rna, dna damage, zinc-finger, dna-binding, photolesion, phosphorylation, misincorporation, rna polymerase ii, transcription-coupled repair, cyclobutane pyrimidine dimer tcr, cpd, arrest, stalling, dna lesion, metal-binding, nuclear protein, transcription bubble, nucleotidyltransferase, damage recognition, elongation complex, transferase, thymine dimer, transcription |
由来する生物種 | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) 詳細 |
細胞内の位置 | Nucleus: P04050 P38902 P08518 P16370 P20433 P20434 P34087 P20436 P27999 Nucleus, nucleolus : P22139 P40422 Cytoplasm : P20435 |
タンパク質・核酸の鎖数 | 15 |
化学式量合計 | 530416.77 |
構造登録者 | Brueckner, F.,Hennecke, U.,Carell, T.,Cramer, P. (登録日: 2006-11-23, 公開日: 2007-02-20, 最終更新日: 2023-12-13) |
主引用文献 | Brueckner, F.,Hennecke, U.,Carell, T.,Cramer, P. Cpd Damage Recognition by Transcribing RNA Polymerase II. Science, 315:859-, 2007 Cited by PubMed Abstract: Cells use transcription-coupled repair (TCR) to efficiently eliminate DNA lesions such as ultraviolet light-induced cyclobutane pyrimidine dimers (CPDs). Here we present the structure-based mechanism for the first step in eukaryotic TCR, CPD-induced stalling of RNA polymerase (Pol) II. A CPD in the transcribed strand slowly passes a translocation barrier and enters the polymerase active site. The CPD 5'-thymine then directs uridine misincorporation into messenger RNA, which blocks translocation. Artificial replacement of the uridine by adenosine enables CPD bypass; thus, Pol II stalling requires CPD-directed misincorporation. In the stalled complex, the lesion is inaccessible, and the polymerase conformation is unchanged. This is consistent with nonallosteric recruitment of repair factors and excision of a lesion-containing DNA fragment in the presence of Pol II. PubMed: 17290000DOI: 10.1126/SCIENCE.1135400 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.8 Å) |
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