1K2E
crystal structure of a nudix protein from Pyrobaculum aerophilum
1K2E の概要
| エントリーDOI | 10.2210/pdb1k2e/pdb |
| 関連するPDBエントリー | 1JRK 1K26 |
| 分子名称 | NUDIX HOMOLOG, SULFATE ION, NICKEL (II) ION, ... (6 entities in total) |
| 機能のキーワード | nudix/mutt-like fold, mixed alpha/beta, dimer, putative nudix hydrolase, structural genomics, unknown function |
| 由来する生物種 | Pyrobaculum aerophilum |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 36609.32 |
| 構造登録者 | Wang, S.,Mura, C.,Sawaya, M.R.,Cascio, D.,Eisenberg, D. (登録日: 2001-09-26, 公開日: 2002-04-03, 最終更新日: 2023-08-16) |
| 主引用文献 | Wang, S.,Mura, C.,Sawaya, M.R.,Cascio, D.,Eisenberg, D. Structure of a Nudix protein from Pyrobaculum aerophilum reveals a dimer with two intersubunit beta-sheets. Acta Crystallogr.,Sect.D, 58:571-578, 2002 Cited by PubMed Abstract: Nudix proteins, formerly called MutT homolog proteins, are a large family of proteins that play an important role in reducing the accumulation of potentially toxic compounds inside the cell. They hydrolyze a wide variety of substrates that are mainly composed of a nucleoside diphosphate linked to some other moiety X and thus are called Nudix hydrolases. Here, the crystal structure of a Nudix hydrolase from the hyperthermophilic archaeon Pyrobaculum aerophilum is reported. The structure was determined by the single-wavelength anomalous scattering method with data collected at the peak anomalous wavelength of an iridium-derivatized crystal. It reveals an extensive dimer interface, with each subunit contributing two strands to the beta-sheet of the other subunit. Individual subunits consist of a mixed highly twisted and curved beta-sheet of 11 beta-strands and two alpha-helices, forming an alpha-beta-alpha sandwich. The conserved Nudix box signature motif, which contains the essential catalytic residues, is located at the first alpha-helix and the beta-strand and loop preceding it. The unusually short connections between secondary-structural elements, together with the dimer form of the structure, are likely to contribute to the thermostability of the P. aerophilum Nudix protein. PubMed: 11914479DOI: 10.1107/S0907444902001191 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.8 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






