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Structural basis for the decarboxylation of orotidine 5'-monophosphate (OMP) by Plasmodium falciparum OMP decarboxylase.
J Biochem. 2008 Jan; 143(1):69-78.JB

Abstract

Orotidine 5'-monophoshate decarboxylase (OMPDC) catalyses 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 A, 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.

Authors+Show Affiliations

Tokuoka K
Department of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan.
Kusakari Y
No affiliation info available
Krungkrai SR
No affiliation info available
Matsumura H
No affiliation info available
Kai Y
No affiliation info available
Krungkrai J
No affiliation info available
Horii T
No affiliation info available
Inoue T
No affiliation info available

MeSH

Amino Acid SequenceAnimalsApoenzymesBinding SitesCrystallography, X-RayDecarboxylationLysineModels, MolecularMolecular Sequence DataOrotidine-5'-Phosphate DecarboxylasePlasmodium falciparumProtein BindingProtein Structure, TertiaryProtozoan ProteinsSequence Homology, Amino AcidUridine Monophosphate

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

17981823

Citation

Tokuoka, Keiji, et al. "Structural Basis for the Decarboxylation of Orotidine 5'-monophosphate (OMP) By Plasmodium Falciparum OMP Decarboxylase." Journal of Biochemistry, vol. 143, no. 1, 2008, pp. 69-78.
Tokuoka K, Kusakari Y, Krungkrai SR, et al. Structural basis for the decarboxylation of orotidine 5'-monophosphate (OMP) by Plasmodium falciparum OMP decarboxylase. J Biochem. 2008;143(1):69-78.
Tokuoka, K., Kusakari, Y., Krungkrai, S. R., Matsumura, H., Kai, Y., Krungkrai, J., Horii, T., & Inoue, T. (2008). Structural basis for the decarboxylation of orotidine 5'-monophosphate (OMP) by Plasmodium falciparum OMP decarboxylase. Journal of Biochemistry, 143(1), 69-78.
Tokuoka K, et al. Structural Basis for the Decarboxylation of Orotidine 5'-monophosphate (OMP) By Plasmodium Falciparum OMP Decarboxylase. J Biochem. 2008;143(1):69-78. PubMed PMID: 17981823.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structural basis for the decarboxylation of orotidine 5'-monophosphate (OMP) by Plasmodium falciparum OMP decarboxylase. AU - Tokuoka,Keiji, AU - Kusakari,Yukiko, AU - Krungkrai,Sudaratana R, AU - Matsumura,Hiroyoshi, AU - Kai,Yasushi, AU - Krungkrai,Jerapan, AU - Horii,Toshihiro, AU - Inoue,Tsuyoshi, Y1 - 2007/11/01/ PY - 2007/11/6/pubmed PY - 2008/7/2/medline PY - 2007/11/6/entrez SP - 69 EP - 78 JF - Journal of biochemistry JO - J Biochem VL - 143 IS - 1 N2 - Orotidine 5'-monophoshate decarboxylase (OMPDC) catalyses 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 A, 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. SN - 0021-924X UR - https://www.unboundmedicine.com/medline/citation/17981823/Structural_basis_for_the_decarboxylation_of_orotidine_5'_monophosphate__OMP__by_Plasmodium_falciparum_OMP_decarboxylase_ DB - PRIME DP - Unbound Medicine ER -