6K3G

Crystal structure of 10-Hydroxygeraniol Dehydrogenase from Cantharanthus roseus in complex with NADP+

6K3G の概要

• エントリーDOI: 10.2210/pdb6k3g/pdb
• 分子名称: 10-hydroxygeraniol oxidoreductase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ZINC ION, ... (4 entities in total)
• 機能のキーワード: 10-hydroxygeraniol, medium chain dehydrogenase/reductase, cantharanthus roseus, mia biosynthesis, oxidoreductase
• 由来する生物種: Catharanthus roseus (Madagascar periwinkle)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39862.34

構造登録者

Sandholu, A.S.,Sharmila, P.M.,Thulasiram, H.V.,Kulkarni, K.A. (登録日: 2019-05-18, 公開日: 2020-03-25, 最終更新日: 2023-11-22)

主引用文献

Sandholu, A.S.,Mujawar, S.P.,Ramakrishnan, K.,Thulasiram, H.V.,Kulkarni, K.
Structural studies on 10-hydroxygeraniol dehydrogenase: A novel linear substrate-specific dehydrogenase from Catharanthus roseus.
Proteins, 88:1197-1206, 2020

PubMed Abstract: Conversion of 10-hydroxygeraniol to 10-oxogeranial is a crucial step in iridoid biosynthesis. This reaction is catalyzed by a zinc-dependent alcohol dehydrogenase, 10-hydroxygeraniol dehydrogenase, belonging to the family of medium-chain dehydrogenase/reductase (MDR). Here, we report the crystal structures of a novel 10-hydroxygeraniol dehydrogenase from Catharanthus roseus in its apo and nicotinamide adenine dinucleotide phosphate (NADP ) bound forms. Structural analysis and docking studies reveal how subtle conformational differences of loops L1, L2, L3, and helix α9' at the orifice of the catalytic site confer differential activity of the enzyme toward various substrates, by modulating the binding pocket shape and volume. The present study, first of its kind, provides insights into the structural basis of substrate specificity of MDRs specific to linear substrates. Furthermore, comparison of apo and NADP bound structures suggests that the enzyme adopts open and closed states to facilitate cofactor binding.

PubMed: 32181958
DOI: 10.1002/prot.25891

実験手法

X-RAY DIFFRACTION (2.41 Å)