2za2: Difference between revisions
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Revision as of 16:31, 6 February 2008
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Crystal Structure of the apo-form of orotidine-5'-monophosphate decarboxylase from P.falciparum
OverviewOverview
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 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.
About this StructureAbout this Structure
2ZA2 is a Single protein structure of sequence from Plasmodium falciparum. Active as Orotidine-5'-phosphate decarboxylase, with EC number 4.1.1.23 Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for the decarboxylation of orotidine 5'-monophosphate (OMP) by Plasmodium falciparum OMP decarboxylase., Tokuoka K, Kusakari Y, Krungkrai SR, Matsumura H, Krungkrai J, Horii T, Inoue T, J Biochem (Tokyo). 2007 Nov 1;. PMID:17981823
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