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Expression, purification, crystallization and preliminary X-ray analysis of perakine reductase, a new member of the aldo-keto reductase enzyme superfamily from higher plants

Abstract

Perakine reductase, a novel member of the aldo-keto reductase enzyme superfamily of higher plants, is involved in the biosynthesis of monoterpenoid indole alkaloids in the Indian medicinal plant Rauvolfia serpentina. The enzyme has been crystallized in C-centered orthorhombic space group and diffracts to 2.0 Å resolution. Perakine reductase (PR) is a novel member of the aldo-keto reductase enzyme superfamily from higher plants. PR from the plant Rauvolfia serpentina is involved in the biosynthesis of monoterpenoid indole alkaloids by performing NADPH-dependent reduction of perakine, yielding raucaffrinoline. However, PR can also reduce cinnamic aldehyde and some of its derivatives. After heterologous expression of a triple mutant of PR in Escherichia coli, crystals of the purified and methylated enzyme were obtained by the hanging-drop vapour-diffusion technique at 293 K with 100 mM sodium citrate pH 5.6 and 27% PEG 4000 as precipitant. Crystals belong to space group C222{sub 1} and diffract to 2.0 Å, with unit-cell parameters a = 58.9, b = 93.0, c = 143.4 Å.
Authors:
Rosenthal, Cindy; [1]  Mueller, Uwe; [2]  Panjikar, Santosh; [3]  Sun, Lianli; [1]  Department of TCM and Natural Drug Research, College of Pharmaceutical Sciences, 513 Zijingang Campus, Zhejiang University, 310058 Hangzhou (China)]; Ruppert, Martin; [1]  Zhao, Yu; [4]  Stöckigt, Joachim; [1]  Department of TCM and Natural Drug Research, College of Pharmaceutical Sciences, 513 Zijingang Campus, Zhejiang University, 310058 Hangzhou (China)]
  1. Department of Pharmaceutical Biology, Institute of Pharmacy, Johannes Gutenberg-University Mainz, Staudinger Weg 5, D-55099 Mainz (Germany)
  2. Berliner Elektronenspeicherring-Gesellschaft für Synchrotronstrahlung mbH, Albert-Einstein-Strasse 15, D-12489 Berlin (Germany)
  3. European Molecular Biology Laboratory Hamburg, Outstation Deutsches Elektronen-Synchrotron, Notkestrasse 85, D-22603 Hamburg (Germany)
  4. Department of TCM and Natural Drug Research, College of Pharmaceutical Sciences, 513 Zijingang Campus, Zhejiang University, 310058 Hangzhou (China)
Publication Date:
Dec 01, 2006
Product Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 62; Journal Issue: Pt 12; Other Information: PMCID: PMC2225361; PMID: 17142919; PUBLISHER-ID: fw5114; OAI: oai:pubmedcentral.nih.gov:2225361; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA)
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; BIOSYNTHESIS; CITRATES; CRYSTALLIZATION; CRYSTALS; DIFFUSION; ESCHERICHIA COLI; REDUCTION; RESOLUTION; SODIUM COMPOUNDS; SPACE GROUPS
OSTI ID:
22356412
Country of Origin:
United Kingdom
Language:
English
Other Identifying Numbers:
Journal ID: ISSN 1744-3091; CODEN: ACSFCL; Other: PII: S174430910605041X; TRN: US15$0830061586
Availability:
Available from http://dx.doi.org/10.1107/S174430910605041X; Available from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2225361
Submitting Site:
USN
Size:
page(s) 1286-1289
Announcement Date:
Jul 17, 2015

Citation Formats

Rosenthal, Cindy, Mueller, Uwe, Panjikar, Santosh, Sun, Lianli, Department of TCM and Natural Drug Research, College of Pharmaceutical Sciences, 513 Zijingang Campus, Zhejiang University, 310058 Hangzhou (China)], Ruppert, Martin, Zhao, Yu, Stöckigt, Joachim, and Department of TCM and Natural Drug Research, College of Pharmaceutical Sciences, 513 Zijingang Campus, Zhejiang University, 310058 Hangzhou (China)]. Expression, purification, crystallization and preliminary X-ray analysis of perakine reductase, a new member of the aldo-keto reductase enzyme superfamily from higher plants. United Kingdom: N. p., 2006. Web. doi:10.1107/S174430910605041X.
Rosenthal, Cindy, Mueller, Uwe, Panjikar, Santosh, Sun, Lianli, Department of TCM and Natural Drug Research, College of Pharmaceutical Sciences, 513 Zijingang Campus, Zhejiang University, 310058 Hangzhou (China)], Ruppert, Martin, Zhao, Yu, Stöckigt, Joachim, & Department of TCM and Natural Drug Research, College of Pharmaceutical Sciences, 513 Zijingang Campus, Zhejiang University, 310058 Hangzhou (China)]. Expression, purification, crystallization and preliminary X-ray analysis of perakine reductase, a new member of the aldo-keto reductase enzyme superfamily from higher plants. United Kingdom. doi:10.1107/S174430910605041X.
Rosenthal, Cindy, Mueller, Uwe, Panjikar, Santosh, Sun, Lianli, Department of TCM and Natural Drug Research, College of Pharmaceutical Sciences, 513 Zijingang Campus, Zhejiang University, 310058 Hangzhou (China)], Ruppert, Martin, Zhao, Yu, Stöckigt, Joachim, and Department of TCM and Natural Drug Research, College of Pharmaceutical Sciences, 513 Zijingang Campus, Zhejiang University, 310058 Hangzhou (China)]. 2006. "Expression, purification, crystallization and preliminary X-ray analysis of perakine reductase, a new member of the aldo-keto reductase enzyme superfamily from higher plants." United Kingdom. doi:10.1107/S174430910605041X. https://www.osti.gov/servlets/purl/10.1107/S174430910605041X.
@misc{etde_22356412,
title = {Expression, purification, crystallization and preliminary X-ray analysis of perakine reductase, a new member of the aldo-keto reductase enzyme superfamily from higher plants}
author = {Rosenthal, Cindy, Mueller, Uwe, Panjikar, Santosh, Sun, Lianli, Department of TCM and Natural Drug Research, College of Pharmaceutical Sciences, 513 Zijingang Campus, Zhejiang University, 310058 Hangzhou (China)], Ruppert, Martin, Zhao, Yu, Stöckigt, Joachim, and Department of TCM and Natural Drug Research, College of Pharmaceutical Sciences, 513 Zijingang Campus, Zhejiang University, 310058 Hangzhou (China)]}
abstractNote = {Perakine reductase, a novel member of the aldo-keto reductase enzyme superfamily of higher plants, is involved in the biosynthesis of monoterpenoid indole alkaloids in the Indian medicinal plant Rauvolfia serpentina. The enzyme has been crystallized in C-centered orthorhombic space group and diffracts to 2.0 Å resolution. Perakine reductase (PR) is a novel member of the aldo-keto reductase enzyme superfamily from higher plants. PR from the plant Rauvolfia serpentina is involved in the biosynthesis of monoterpenoid indole alkaloids by performing NADPH-dependent reduction of perakine, yielding raucaffrinoline. However, PR can also reduce cinnamic aldehyde and some of its derivatives. After heterologous expression of a triple mutant of PR in Escherichia coli, crystals of the purified and methylated enzyme were obtained by the hanging-drop vapour-diffusion technique at 293 K with 100 mM sodium citrate pH 5.6 and 27% PEG 4000 as precipitant. Crystals belong to space group C222{sub 1} and diffract to 2.0 Å, with unit-cell parameters a = 58.9, b = 93.0, c = 143.4 Å.}
doi = {10.1107/S174430910605041X}
journal = {Acta Crystallographica. Section F}
issue = {Pt 12}
volume = {62}
journal type = {AC}
place = {United Kingdom}
year = {2006}
month = {Dec}
}