2za3: Difference between revisions
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|PDB= 2za3 |SIZE=350|CAPTION= <scene name='initialview01'>2za3</scene>, resolution 2.65Å | |PDB= 2za3 |SIZE=350|CAPTION= <scene name='initialview01'>2za3</scene>, resolution 2.65Å | ||
|SITE= <scene name='pdbsite=AC1:U5p+Binding+Site+For+Residue+A+500'>AC1</scene> and <scene name='pdbsite=AC2:U5p+Binding+Site+For+Residue+B+600'>AC2</scene> | |SITE= <scene name='pdbsite=AC1:U5p+Binding+Site+For+Residue+A+500'>AC1</scene> and <scene name='pdbsite=AC2:U5p+Binding+Site+For+Residue+B+600'>AC2</scene> | ||
|LIGAND= <scene name='pdbligand=U5P:URIDINE-5 | |LIGAND= <scene name='pdbligand=U5P:URIDINE-5'-MONOPHOSPHATE'>U5P</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= [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] | ||
|GENE= | |GENE= | ||
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[[Category: uridine 5'-monophosphate]] | [[Category: uridine 5'-monophosphate]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 15:57:04 2008'' | ||
Revision as of 13:57, 23 March 2008
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| 2za3, resolution 2.65Å | |||||||||||||
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| Sites: | AC1 and AC2 | ||||||||||||
| Ligands: | U5P | ||||||||||||
| Activity: | Orotidine-5'-phosphate decarboxylase, with EC number 4.1.1.23 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Crystal Structure of orotidine 5'-monophosphate decarboxylase complexed with uridine 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
2ZA3 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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