3I1C

Crystal Structure of a Novel Engineered Diels-Alderase: DA_20_00_A74I

3I1C の概要

• エントリーDOI: 10.2210/pdb3i1c/pdb
• 分子名称: Diisopropyl-fluorophosphatase, GLYCEROL (3 entities in total)
• 機能のキーワード: beta-propeller, hydrolase, metal-binding
• 由来する生物種: Loligo vulgaris (Common European squid)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36194.11

構造登録者

Lambert, A.R.,Stoddard, B.L. (登録日: 2009-06-26, 公開日: 2009-08-18, 最終更新日: 2024-02-21)

主引用文献

Siegel, J.B.,Zanghellini, A.,Lovick, H.M.,Kiss, G.,Lambert, A.R.,St Clair, J.L.,Gallaher, J.L.,Hilvert, D.,Gelb, M.H.,Stoddard, B.L.,Houk, K.N.,Michael, F.E.,Baker, D.
Computational design of an enzyme catalyst for a stereoselective bimolecular Diels-Alder reaction.
Science, 329:309-313, 2010

PubMed Abstract: The Diels-Alder reaction is a cornerstone in organic synthesis, forming two carbon-carbon bonds and up to four new stereogenic centers in one step. No naturally occurring enzymes have been shown to catalyze bimolecular Diels-Alder reactions. We describe the de novo computational design and experimental characterization of enzymes catalyzing a bimolecular Diels-Alder reaction with high stereoselectivity and substrate specificity. X-ray crystallography confirms that the structure matches the design for the most active of the enzymes, and binding site substitutions reprogram the substrate specificity. Designed stereoselective catalysts for carbon-carbon bond-forming reactions should be broadly useful in synthetic chemistry.

PubMed: 20647463
DOI: 10.1126/science.1190239

実験手法

X-RAY DIFFRACTION (2.2 Å)