2za3: Difference between revisions

Revision as of 20:01, 21 February 2008

Crystal Structure of orotidine 5'-monophosphate decarboxylase complexed with uridine 5'-monophosphate from P.falciparum

OverviewOverview

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.

About this StructureAbout 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 Known structural/functional Sites: and . 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, Kai Y, Krungkrai J, Horii T, Inoue T, J Biochem. 2008 Jan;143(1):69-78. Epub 2007 Nov 1. PMID:17981823

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 ==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.
+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.
 ==About this Structure==
@@ Line 10: / Line 10: @@
 ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17981823 17981823]
+Structural Basis for the Decarboxylation of Orotidine 5'-Monophosphate (OMP) by Plasmodium Falciparum OMP Decarboxylase., Tokuoka K, Kusakari Y, Krungkrai SR, Matsumura H, Kai Y, Krungkrai J, Horii T, Inoue T, J Biochem. 2008 Jan;143(1):69-78. Epub 2007 Nov 1. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17981823 17981823]
 [[Category: Orotidine-5'-phosphate decarboxylase]]
 [[Category: Plasmodium falciparum]]
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 [[Category: uridine 5'-monophosphate]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 13 08:13:34 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:01:04 2008''