1p6o
From Proteopedia
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The crystal structure of yeast cytosine deaminase bound to 4(R)-hydroxyl-3,4-dihydropyrimidine at 1.14 angstroms.
Overview
Cytosine deaminase (CD) catalyzes the deamination of cytosine and is only present in prokaryotes and fungi, where it is a member of the pyrimidine salvage pathway. The enzyme is of interest both for antimicrobial drug design and gene therapy applications against tumors. The structure of Saccharomyces cerevisiae CD has been determined in the presence and absence of a mechanism-based inhibitor, at 1.14 and 1.43 A resolution, respectively. The enzyme forms an alpha/beta fold similar to bacterial cytidine deaminase, but with no similarity to the alpha/beta barrel fold used by bacterial cytosine deaminase or mammalian adenosine deaminase. The structures observed for bacterial, fungal, and mammalian nucleic acid deaminases represent an example of the parallel evolution of two unique protein folds to carry out the same reaction on a diverse array of substrates.
About this Structure
1P6O is a Single protein structure of sequence from Saccharomyces cerevisiae with , , and as ligands. Active as Cytosine deaminase, with EC number 3.5.4.1 Full crystallographic information is available from OCA.
Reference
The 1.14 A crystal structure of yeast cytosine deaminase: evolution of nucleotide salvage enzymes and implications for genetic chemotherapy., Ireton GC, Black ME, Stoddard BL, Structure. 2003 Aug;11(8):961-72. PMID:12906827
Page seeded by OCA on Thu Feb 21 14:25:43 2008
Categories: Cytosine deaminase | Saccharomyces cerevisiae | Single protein | Black, M E. | Ireton, G C. | Stoddard, B L. | ACY | CA | HPY | ZN | Dimer | Hydrolase | Inhibitor bound
