1YGZ
Crystal Structure of Inorganic Pyrophosphatase from Helicobacter pylori
1YGZ の概要
| エントリーDOI | 10.2210/pdb1ygz/pdb |
| 分子名称 | Inorganic pyrophosphatase (2 entities in total) |
| 機能のキーワード | hydrolase |
| 由来する生物種 | Helicobacter pylori |
| 細胞内の位置 | Cytoplasm (By similarity): P56153 |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 116913.12 |
| 構造登録者 | Wu, C.A.,Lokanath, N.K.,Kim, D.Y.,Park, H.J.,Hwang, H.Y.,Kim, S.T.,Suh, S.W.,Kim, K.K. (登録日: 2005-01-06, 公開日: 2005-11-01, 最終更新日: 2024-10-30) |
| 主引用文献 | Wu, C.A.,Lokanath, N.K.,Kim, D.Y.,Park, H.J.,Hwang, H.Y.,Kim, S.T.,Suh, S.W.,Kim, K.K. Structure of inorganic pyrophosphatase from Helicobacter pylori. Acta Crystallogr.,Sect.D, 61:1459-1464, 2005 Cited by PubMed Abstract: Inorganic pyrophosphatase (PPase) is a ubiquitous cytosolic enzyme which catalyzes the hydrolysis of inorganic pyrophosphate (PPi) to orthophosphate (Pi). The crystal structure of inorganic pyrophosphatase from Helicobacter pylori (H-PPase) has been solved by MAD and refined to an R factor of 20.6% at 2.6 A resolution. The crystallographic asymmetric unit contains a homohexameric H-PPase arranged as a dimer of trimers. While most of the structural elements of PPases are highly conserved in H-PPase, some unique structural features are localized in the flexible loops near the active site, suggesting that the structural flexibility of these loops is required for the catalytic efficiency of PPase. PubMed: 16239722DOI: 10.1107/S0907444905025667 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.6 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






