1E0J
gp4d helicase from phage T7 ADPNP complex
1E0J の概要
| エントリーDOI | 10.2210/pdb1e0j/pdb |
| 関連するPDBエントリー | 1B79 1CR0 1CR1 1CR2 1CR4 1E0K 1JWE |
| 分子名称 | DNA HELICASE, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION (3 entities in total) |
| 機能のキーワード | helicase, atpase, dna replication |
| 由来する生物種 | PHAGE T7 |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 192652.84 |
| 構造登録者 | Singleton, M.R.,Sawaya, M.R.,Ellenberger, T.,Wigley, D.B. (登録日: 2000-03-30, 公開日: 2000-06-09, 最終更新日: 2024-05-08) |
| 主引用文献 | Singleton, M.R.,Sawaya, M.R.,Ellenberger, T.,Wigley, D.B. Crystal Structure of T7 Gene 4 Ring Helicase Indicates a Mechanism for Sequential Hydrolysis of Nucleotides Cell(Cambridge,Mass.), 101:589-, 2000 Cited by PubMed Abstract: We have determined the crystal structure of an active, hexameric fragment of the gene 4 helicase from bacteriophage T7. The structure reveals how subunit contacts stabilize the hexamer. Deviation from expected six-fold symmetry of the hexamer indicates that the structure is of an intermediate on the catalytic pathway. The structural consequences of the asymmetry suggest a "binding change" mechanism to explain how cooperative binding and hydrolysis of nucleotides are coupled to conformational changes in the ring that most likely accompany duplex unwinding. The structure of a complex with a nonhydrolyzable ATP analog provides additional evidence for this hypothesis, with only four of the six possible nucleotide binding sites being occupied in this conformation of the hexamer. This model suggests a mechanism for DNA translocation. PubMed: 10892646DOI: 10.1016/S0092-8674(00)80871-5 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3 Å) |
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