3T15
Structure of green-type Rubisco activase from tobacco
3T15 の概要
| エントリーDOI | 10.2210/pdb3t15/pdb |
| 関連するPDBエントリー | 3zw6 |
| EMDBエントリー | 1940 |
| 分子名称 | Ribulose bisphosphate carboxylase/oxygenase activase 1, chloroplastic (1 entity in total) |
| 機能のキーワード | photosynthesis, rubisco activase, aaa+ protein |
| 由来する生物種 | Nicotiana tabacum (American tobacco,tobacco) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 32856.80 |
| 構造登録者 | Stotz, M.,Wendler, P.,Mueller-Cajar, O.,Hartl, F.U.,Bracher, A.,Hayer-Hartl, M. (登録日: 2011-07-21, 公開日: 2011-11-09, 最終更新日: 2024-02-28) |
| 主引用文献 | Stotz, M.,Mueller-Cajar, O.,Ciniawsky, S.,Wendler, P.,Hartl, F.U.,Bracher, A.,Hayer-Hartl, M. Structure of green-type Rubisco activase from tobacco. Nat.Struct.Mol.Biol., 18:1366-1370, 2011 Cited by PubMed Abstract: Rubisco, the enzyme that catalyzes the fixation of atmospheric CO(2) in photosynthesis, is subject to inactivation by inhibitory sugar phosphates. Here we report the 2.95-Å crystal structure of Nicotiana tabacum Rubisco activase (Rca), the enzyme that facilitates the removal of these inhibitors. Rca from tobacco has a classical AAA(+)-protein domain architecture. Although Rca populates a range of oligomeric states when in solution, it forms a helical arrangement with six subunits per turn when in the crystal. However, negative-stain electron microscopy of the active mutant R294V suggests that Rca functions as a hexamer. The residues determining species specificity for Rubisco are located in a helical insertion of the C-terminal domain and probably function in conjunction with the N-domain in Rubisco recognition. Loop segments exposed toward the central pore of the hexamer are required for the ATP-dependent remodeling of Rubisco, resulting in the release of inhibitory sugar. PubMed: 22056769DOI: 10.1038/nsmb.2171 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.95 Å) |
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