1JCL

OBSERVATION OF COVALENT INTERMEDIATES IN AN ENZYME MECHANISM AT ATOMIC RESOLUTION

1JCL の概要

• エントリーDOI: 10.2210/pdb1jcl/pdb
• 関連するPDBエントリー: 1JCJ
• 分子名称: DEOXYRIBOSE-PHOSPHATE ALDOLASE, 1-HYDROXY-PENTANE-3,4-DIOL-5-PHOSPHATE (3 entities in total)
• 機能のキーワード: alpha-beta tim barrel, lyase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P0A6L0
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 56246.18

構造登録者

Heine, A.,DeSantis, G.,Luz, J.G.,Mitchell, M.,Wong, C.-H.,Wilson, I.A. (登録日: 2001-06-09, 公開日: 2001-10-31, 最終更新日: 2024-11-20)

主引用文献

Heine, A.,DeSantis, G.,Luz, J.G.,Mitchell, M.,Wong, C.H.,Wilson, I.A.
Observation of covalent intermediates in an enzyme mechanism at atomic resolution.
Science, 294:369-374, 2001

PubMed Abstract: In classical enzymology, intermediates and transition states in a catalytic mechanism are usually inferred from a series of biochemical experiments. Here, we derive an enzyme mechanism from true atomic-resolution x-ray structures of reaction intermediates. Two ultra-high resolution structures of wild-type and mutant d-2-deoxyribose-5-phosphate (DRP) aldolase complexes with DRP at 1.05 and 1.10 angstroms unambiguously identify the postulated covalent carbinolamine and Schiff base intermediates in the aldolase mechanism. In combination with site-directed mutagenesis and (1)H nuclear magnetic resonance, we can now propose how the heretofore elusive C-2 proton abstraction step and the overall stereochemical course are accomplished. A proton relay system appears to activate a conserved active-site water that functions as the critical mediator for proton transfer.

PubMed: 11598300
DOI: 10.1126/science.1063601

実験手法

X-RAY DIFFRACTION (1.05 Å)