3Q0A
X-ray crystal structure of the transcription initiation complex of the N4 mini-vRNAP with P2 promoter: Mismatch complex
3Q0A の概要
エントリーDOI | 10.2210/pdb3q0a/pdb |
関連するPDBエントリー | 3Q22 3Q23 3Q24 |
分子名称 | Virion RNA polymerase, DNA (5'-D(*TP*GP*CP*CP*TP*CP*CP*CP*AP*GP*GP*CP*A*GP*TP*CP*AP*AP*AP*AP*GP*AP*AP*GP*CP*GP*GP*AP*GP*CP*TP*TP*CP*TP*TP*C)-3'), PHOSPHATE ION, ... (5 entities in total) |
機能のキーワード | rna polymerase, transcription-dna complex, transcription/dna |
由来する生物種 | Enterobacteria phage N4 (Bacteriophage N4) |
細胞内の位置 | Virion : Q859P9 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 269717.53 |
構造登録者 | |
主引用文献 | Gleghorn, M.L.,Davydova, E.K.,Basu, R.,Rothman-Denes, L.B.,Murakami, K.S. X-ray crystal structures elucidate the nucleotidyl transfer reaction of transcript initiation using two nucleotides. Proc.Natl.Acad.Sci.USA, 108:3566-3571, 2011 Cited by PubMed Abstract: We have determined the X-ray crystal structures of the pre- and postcatalytic forms of the initiation complex of bacteriophage N4 RNA polymerase that provide the complete set of atomic images depicting the process of transcript initiation by a single-subunit RNA polymerase. As observed during T7 RNA polymerase transcript elongation, substrate loading for the initiation process also drives a conformational change of the O-helix, but only the correct base pairing between the +2 substrate and DNA base is able to complete the O-helix conformational transition. Substrate binding also facilitates catalytic metal binding that leads to alignment of the reactive groups of substrates for the nucleotidyl transfer reaction. Although all nucleic acid polymerases use two divalent metals for catalysis, they differ in the requirements and the timing of binding of each metal. In the case of bacteriophage RNA polymerase, we propose that catalytic metal binding is the last step before the nucleotidyl transfer reaction. PubMed: 21321236DOI: 10.1073/pnas.1016691108 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.69 Å) |
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