1AUS

ACTIVATED UNLIGANDED SPINACH RUBISCO

1AUS の概要

• エントリーDOI: 10.2210/pdb1aus/pdb
• 分子名称: RIBULOSE BISPHOSPHATE CARBOXYLASE/OXYGENASE, MAGNESIUM ION, FORMIC ACID, ... (5 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 Q43832
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 269774.72

構造登録者

Taylor, T.C.,Andersson, I. (登録日: 1995-06-21, 公開日: 1995-10-15, 最終更新日: 2025-03-26)

主引用文献

Taylor, T.C.,Andersson, I.
Structure of a product complex of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase.
Biochemistry, 36:4041-4046, 1997

PubMed Abstract: The crystal structure of an activated complex of ribulose-1,5-bisphosphate carboxylase/oxygenase from spinach and its product 3-phosphoglycerate has been determined to 2.2 A resolution. The structure is of the open form with the active site accessible to the solvent as observed in the structures of the activated ligand-free enzyme and the complex of the activated enzyme with the substrate ribulose-1,5-bisphosphate. Two molecules of 3-phosphoglycerate are bound per active site. The phosphates of both molecules bind approximately at the same position as the phosphates of ribulose-1,5-bisphosphate or the six-carbon intermediate analogue 2-carboxyarabinitol-1,5-bisphosphate, but one product molecule is swung out from the active site with its carboxylate group pointing toward solution. The present structure points to direct participation of the active site side chain of lysine 175 in later stages of catalysis. This possibility is discussed in the light of mutagenesis studies.

PubMed: 9092835
DOI: 10.1021/bi962818w

実験手法

X-RAY DIFFRACTION (2.2 Å)