1RCO
SPINACH RUBISCO IN COMPLEX WITH THE INHIBITOR D-XYLULOSE-2,2-DIOL-1,5-BISPHOSPHATE
1RCO の概要
エントリーDOI | 10.2210/pdb1rco/pdb |
分子名称 | RIBULOSE BISPHOSPHATE CARBOXYLASE/OXYGENASE, D-XYLULOSE-2,2-DIOL-1,5-BISPHOSPHATE, ... (4 entities in total) |
機能のキーワード | lyase, carbon-carbon |
由来する生物種 | Spinacia oleracea (spinach) 詳細 |
細胞内の位置 | Plastid, chloroplast: P00875 P00870 |
タンパク質・核酸の鎖数 | 16 |
化学式量合計 | 541611.65 |
構造登録者 | |
主引用文献 | Taylor, T.C.,Fothergill, M.D.,Andersson, I. A common structural basis for the inhibition of ribulose 1,5-bisphosphate carboxylase by 4-carboxyarabinitol 1,5-bisphosphate and xylulose 1,5-bisphosphate. J.Biol.Chem., 271:32894-32899, 1996 Cited by PubMed Abstract: Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyzes the carboxylation of ribulose 1,5-bisphosphate. The reaction catalyzed by Rubisco involves several steps, some of which can occur as partial reactions, forming intermediates that can be isolated. Analogues of these intermediates are potent inhibitors of the enzyme. We have studied the interactions with the enzyme of two inhibitors, xylulose 1,5-bisphosphate and 4-carboxyarabinitol 1,5-bisphosphate, by x-ray crystallography. Crystals of the complexes were formed by cocrystallization under activating conditions. In addition, 4-carboxyarabinitol 1,5-bisphosphate was soaked into preformed activated crystals of the enzyme. The result of these experiments was the release of the activating CO2 molecule as well as the metal ion from the active site when the inhibitors bound to the enzyme. Comparison with the structure of an activated complex of the enzyme indicates that the structural basis for the release of the activator groups is a distortion of the metal binding site due to the different geometry of the C-3 hydroxyl of the inhibitors. Both inhibitors induce closure of active site loops despite the inactivated state of the enzyme. Xylulose 1,5-bisphosphate binds in a hydrated form at the active site. PubMed: 8955130DOI: 10.1074/jbc.271.51.32894 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.3 Å) |
構造検証レポート
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