2za1

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

spinqualitylabelsall models 2za1, resolution 2.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2za1 is a 2 chain structure with sequence from Plasmodium falciparum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.65Å Ligands: OMP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8T6J6_PLAFA Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Uridine 5'-monophosphate synthase 3D structures

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