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Journal of Biochemistry Advance Access published online on November 1, 2007
Journal of Biochemistry, doi:10.1093/jb/mvm193
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© 2007 The Japanese Biochemical Society

Structural basis for the decarboxylation of orotidine 5'-monophosphate (OMP) by Plasmodium falciparum OMP decarboxylase

Keiji Tokuoka2, Yukiko Kusakari2, Sudaratana R. Krungkrai3,4, Hiroyoshi Matsumura2, Jerapan Krungkrai5, Toshihiro Horii3 and Tsuyoshi Inoue*,2

2 Department of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan
3 Department of Molecular Protozoology, Research Institute for Microbial Diseases, Osaka University, 3-1 Yamadaoka, Suita, Osaka 565-0871, Japan
4 Unit of Biochemistry, Department of Medical Science, Faculty of Science, Rangsit University, Patumthani 12000, Thailand
5 Department of Biochemistry, Faculty of Medicine, Chulalongkorn University, Rama IV Road, Bangkok 10330, Thailand

Corresponding author: * Dr. Tsuyoshi Inoue, Tel: +81-6-6879-7410, Fax: +81-6-6879-7409, E-mail: inouet{at}chem.eng.osaka-u.ac.jp

Received August 6, 2007; Accepted October 2, 2007


  Abstract

Summary

Orotidine 5'-monophoshate decarboxylase (OMPDC) catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). Here, we report the X-ray analysis of apo, substrate or product-complex forms of OMPDC from Plasmodium falciparum (PfOMPDC) at 2.7, 2.65 and 2.65 Å, respectively. The structural analysis provides the substrate recognition mechanism with dynamic structural changes, as well as the rearrangement of the hydrogen bond array at the active site. The structural basis of substrate or product binding to PfOMPDC will help to uncover the decarboxylation mechanism and facilitate structure-based optimization of antimalarial drugs.

Key Words: Orotidine 5'-monophoshate decarboxylase, x-ray structural analysis, apo form, OMP-complex, UMP-complex, structural comparison


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