1S76
T7 RNA polymerase alpha beta methylene ATP elongation complex
1S76 の概要
エントリーDOI | 10.2210/pdb1s76/pdb |
分子名称 | DNA (5'-D(P*GP*CP*CP*GP*TP*GP*CP*GP*CP*AP*TP*TP*CP*GP*CP*CP*GP*TP*GP*TP*T)-3'), DNA (5'-D(P*TP*TP*TP*AP*CP*GP*TP*TP*GP*CP*GP*CP*AP*CP*GP*GP*C)-3'), RNA (5'-R(P*AP*CP*AP*CP*GP*GP*CP*GP*A)-3'), ... (6 entities in total) |
機能のキーワード | t7 rna polymerase, transferase |
由来する生物種 | Enterobacteria phage T7 詳細 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 114048.35 |
構造登録者 | |
主引用文献 | Yin, Y.W.,Steitz, T.A. The structural mechanism of translocation and helicase activity in T7 RNA polymerase. Cell(Cambridge,Mass.), 116:393-404, 2004 Cited by PubMed Abstract: RNA polymerase functions like a molecular motor that can convert chemical energy into the work of strand separation and translocation along the DNA during transcription. The structures of phage T7 RNA polymerase in an elongation phase substrate complex that includes the incoming nucleoside triphosphate and a pretranslocation product complex that includes the product pyrophosphate (PPi) are described here. These structures and the previously determined posttranslocation elongation complex demonstrate that two enzyme conformations exist during a cycle of single nucleotide addition. One orientation of a five-helix subdomain is stabilized by the phosphates of either the incoming NTP or by the product PPi. A second orientation of this subdomain is stable in their absence and is associated with translocation of the heteroduplex product as well as strand separation of the downstream DNA. We propose that the dissociation of the product PPi after nucleotide addition produces the protein conformational change resulting in translocation and strand separation. PubMed: 15016374DOI: 10.1016/S0092-8674(04)00120-5 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.88 Å) |
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