Crystallization and preliminary X‐ray diffraction analysis of (R)‐carbonyl reductase from Candida parapsilosis. Issue 6 (1st June 2014)

• Record Type: Journal Article
• Authors: Wang, Shanshan; Nie, Yao; Yan, Xu; Ko, Tzu‐Ping; Huang, Chun‐Hsiang; Chan, Hsiu‐Chien; Guo, Rey‐Ting; Xiao, Rong
• Is Part Of: Acta crystallographica. Volume 70:Issue 6(2014:Jun.)
• Page Start: 800
• Page End: 802
• Publication Date: 2014-06-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X1400908X
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The NADH‐dependent (<italic>R</italic>)‐carbonyl reductase from <italic>Candida parapsilosis</italic> (RCR) catalyzes the asymmetric reduction of 2‐hydroxyacetophenone (HAP) to produce (<italic>R</italic>)‐1‐phenyl‐1, 2‐ethanediol [(<italic>R</italic>)‐PED], which is used as a versatile building block for the synthesis of pharmaceuticals and fine chemicals. To gain insight into the catalytic mechanism, the structures of complexes of RCR with ligands, including the coenzyme, are important. Here, the recombinant RCR protein was expressed and purified in <italic>Escherichia coli</italic> and was crystallized in the presence of NAD⁺. The crystals, which belonged to the orthorhombic space group <italic>P</italic>2₁2₁2₁, with unit‐cell parameters <italic>a</italic> = 85.64, <italic>b</italic> = 106.11, <italic>c</italic> = 145.55 Å, were obtained by the sitting‐drop vapour‐diffusion method and diffracted to 2.15 Å resolution. Initial model building indicates that RCR forms a homotetramer, consistent with previous reports of medium‐chain‐type alcohol dehydrogenases.</p> </abstract>