1RLC

CRYSTAL STRUCTURE OF THE UNACTIVATED RIBULOSE 1, 5-BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE COMPLEXED WITH A TRANSITION STATE ANALOG, 2-CARBOXY-D-ARABINITOL 1,5-BISPHOSPHATE

1RLC の概要

• エントリーDOI: 10.2210/pdb1rlc/pdb
• 分子名称: RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE/OXYGENASE (LARGE CHAIN), RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE/OXYGENASE (SMALL CHAIN), 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: lyase(carbon-carbon)
• 由来する生物種: Nicotiana tabacum (common tobacco); 詳細
• 細胞内の位置: Plastid, chloroplast: P69249
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 67896.79

構造登録者

Zhang, K.Y.J.,Cascio, D.,Eisenberg, D. (登録日: 1993-08-04, 公開日: 1993-10-31, 最終更新日: 2024-10-30)

主引用文献

Zhang, K.Y.,Cascio, D.,Eisenberg, D.
Crystal structure of the unactivated ribulose 1,5-bisphosphate carboxylase/oxygenase complexed with a transition state analog, 2-carboxy-D-arabinitol 1,5-bisphosphate.
Protein Sci., 3:64-69, 1994

PubMed Abstract: The crystal structure of unactivated ribulose 1,5-bisphosphate carboxylase/oxygenase from Nicotiana tabacum complexed with a transition state analog, 2-carboxy-D-arabinitol 1,5-bisphosphate, was determined to 2.7 A resolution by X-ray crystallography. The transition state analog binds at the active site in an extended conformation. As compared to the binding of the same analog in the activated enzyme, the analog binds in a reverse orientation. The active site Lys 201 is within hydrogen bonding distance of the carboxyl oxygen of the analog. Loop 6 (residues 330-339) remains open and flexible upon binding of the analog in the unactivated enzyme, in contrast to the closed and ordered loop 6 in the activated enzyme complex. The transition state analog is exposed to solvent due to the open conformation of loop 6.

PubMed: 8142899

実験手法

X-RAY DIFFRACTION (2.7 Å)