2za3
From Proteopedia
(New page: 200px<br /><applet load="2za3" size="350" color="white" frame="true" align="right" spinBox="true" caption="2za3, resolution 2.65Å" /> '''Crystal Structure of...) |
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Revision as of 13:32, 6 February 2008
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Crystal Structure of orotidine 5'-monophosphate decarboxylase complexed with uridine 5'-monophosphate from P.falciparum
Overview
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 Structure
2ZA3 is a Single protein structure of sequence from Plasmodium falciparum with as ligand. Active as Orotidine-5'-phosphate decarboxylase, with EC number 4.1.1.23 Full crystallographic information is available from OCA.
Reference
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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