6KJ5

Crystal structure of 10-Hydroxygeraniol Dehydrogenase apo form from Cantharanthus roseus

Summary for 6KJ5

• Entry DOI: 10.2210/pdb6kj5/pdb
• Descriptor: 10-hydroxygeraniol dehydrogenase, ZINC ION (2 entities in total)
• Functional Keywords: 10-hydroxygeraniol, medium chain dehydrogenase/reductase, cantharanthus roseus, mia biosynthesis, oxidoreductase
• Biological source: Catharanthus roseus (Madagascar periwinkle)
• Total number of polymer chains: 1
• Total formula weight: 38716.40

Authors

Sandholu, A.S.,Sharmila, P.M.,Thulasiram, H.V.,Kulkarni, K.A. (deposition date: 2019-07-21, release date: 2020-03-25, Last modification date: 2023-11-22)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.75 Å)