3ORY
Crystal structure of Flap endonuclease 1 from hyperthermophilic archaeon Desulfurococcus amylolyticus
3ORY の概要
| エントリーDOI | 10.2210/pdb3ory/pdb |
| 分子名称 | flap endonuclease 1, PHOSPHATE ION (3 entities in total) |
| 機能のキーワード | endonuclease, hydrolase |
| 由来する生物種 | Desulfurococcus amylolyticus |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 41164.02 |
| 構造登録者 | Mase, T.,Kubota, K.,Miyazono, K.,Kawarabayashii, Y.,Tanokura, M. (登録日: 2010-09-08, 公開日: 2011-02-09, 最終更新日: 2024-03-20) |
| 主引用文献 | Mase, T.,Kubota, K.,Miyazono, K.,Kawarabayasi, Y.,Tanokura, M. Structure of flap endonuclease 1 from the hyperthermophilic archaeon Desulfurococcus amylolyticus Acta Crystallogr.,Sect.F, 67:209-213, 2011 Cited by PubMed Abstract: Flap endonuclease 1 (FEN1) is a key enzyme in DNA repair and DNA replication. It is a structure-specific nuclease that removes 5'-overhanging flaps and the RNA/DNA primer during maturation of the Okazaki fragment. Homologues of FEN1 exist in a wide range of bacteria, archaea and eukaryotes. In order to further understand the structural basis of the DNA recognition, binding and cleavage mechanism of FEN1, the structure of FEN1 from the hyperthermophilic archaeon Desulfurococcus amylolyticus (DaFEN1) was determined at 2.00 Å resolution. The overall fold of DaFEN1 was similar to those of other archaeal FEN1 proteins; however, the helical clamp and the flexible loop exhibited a putative substrate-binding pocket with a unique conformation. PubMed: 21301087DOI: 10.1107/S1744309110053030 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2 Å) |
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