2za2

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[[Category: pyrimidine biosynthesis]]
[[Category: pyrimidine biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 6 15:31:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 6 17:29:23 2008''

Revision as of 15:29, 6 February 2008


2za2, resolution 2.70Å

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Crystal Structure of the apo-form of orotidine-5'-monophosphate decarboxylase 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

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.

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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