1N1H
Initiation complex of polymerase lambda3 from reovirus
1N1H の概要
エントリーDOI | 10.2210/pdb1n1h/pdb |
関連するPDBエントリー | 1MUK 1MWH |
分子名称 | 5'-R(*AP*UP*UP*AP*GP*C)-3', Minor core protein lambda 3, MANGANESE (II) ION, ... (8 entities in total) |
機能のキーワード | polymerase, initiation complex, right hand configuration, transferase-rna complex, transferase/rna |
由来する生物種 | Mammalian orthoreovirus 3 詳細 |
細胞内の位置 | Virion (Potential): P17378 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 146205.64 |
構造登録者 | Tao, Y.,Farsetta, D.L.,Nibert, M.L.,Harrison, S.C. (登録日: 2002-10-17, 公開日: 2002-12-25, 最終更新日: 2024-04-03) |
主引用文献 | Tao, Y.,Farsetta, D.L.,Nibert, M.L.,Harrison, S.C. RNA Synthesis in a Cage--Structural Studies of Reovirus Polymerase [lambda] 3 Cell(Cambridge,Mass.), 111:733-745, 2002 Cited by PubMed Abstract: The reovirus polymerase and those of other dsRNA viruses function within the confines of a protein capsid to transcribe the tightly packed dsRNA genome segments. The crystal structure of the reovirus polymerase, lambda3, determined at 2.5 A resolution, shows a fingers-palm-thumb core, similar to those of other viral polymerases, surrounded by major N- and C-terminal elaborations, which create a cage-like structure, with four channels leading to the catalytic site. This "caged" polymerase has allowed us to visualize the results of several rounds of RNA polymerization directly in the crystals. A 5' cap binding site on the surface of lambda3 suggests a template retention mechanism by which attachment of the 5' end of the plus-sense strand facilitates insertion of the 3' end of the minus-sense strand into the template channel. PubMed: 12464184DOI: 10.1016/S0092-8674(02)01110-8 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.8 Å) |
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