2za1: Difference between revisions

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|SITE= <scene name='pdbsite=AC1:Omp+Binding+Site+For+Residue+A+500'>AC1</scene> and <scene name='pdbsite=AC2:Omp+Binding+Site+For+Residue+B+600'>AC2</scene>
|SITE= <scene name='pdbsite=AC1:Omp+Binding+Site+For+Residue+A+500'>AC1</scene> and <scene name='pdbsite=AC2:Omp+Binding+Site+For+Residue+B+600'>AC2</scene>
|LIGAND= <scene name='pdbligand=OMP:OROTIDINE-5&#39;-MONOPHOSPHATE'>OMP</scene>
|LIGAND= <scene name='pdbligand=OMP:OROTIDINE-5&#39;-MONOPHOSPHATE'>OMP</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Orotidine-5'-phosphate_decarboxylase Orotidine-5'-phosphate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.23 4.1.1.23]  
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Orotidine-5'-phosphate_decarboxylase Orotidine-5'-phosphate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.23 4.1.1.23] </span>
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=[[2f84|2F84]], [[2za2|2ZA2]], [[2za3|2ZA3]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2za1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2za1 OCA], [http://www.ebi.ac.uk/pdbsum/2za1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2za1 RCSB]</span>
}}
}}


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[[Category: Inoue, T.]]
[[Category: Inoue, T.]]
[[Category: Tokuoka, K.]]
[[Category: Tokuoka, K.]]
[[Category: OMP]]
[[Category: lyase]]
[[Category: lyase]]
[[Category: orotidine 5'-monophosphate]]
[[Category: orotidine 5'-monophosphate]]
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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 Mon Mar 31 05:19:50 2008''

Revision as of 02:19, 31 March 2008

File:2za1.jpg


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2za1, resolution 2.65Å
Sites: AC1 and AC2
Ligands: OMP
Activity: Orotidine-5'-phosphate decarboxylase, with EC number 4.1.1.23
Related: 2F84, 2ZA2, 2ZA3


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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


Overview

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

2ZA1 is a Single protein structure of sequence from Plasmodium falciparum. 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, 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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