1OX7

Crystal structure of yeast cytosine deaminase apo-enzyme: inorganic zinc bound

Summary for 1OX7

• Entry DOI: 10.2210/pdb1ox7/pdb
• Descriptor: Cytosine deaminase, ZINC ION, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: aminohydrolase, hydrolase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 2
• Total formula weight: 36480.70

Authors

Ireton, G.C.,Black, M.E.,Stoddard, B.L. (deposition date: 2003-04-01, release date: 2003-08-19, Last modification date: 2011-07-13)

Primary citation

Ireton, G.C.,Black, M.E.,Stoddard, B.L.
The 1.14 a crystal structure of yeast Cytosine deaminase. Evolution of nucleotide salvage enzymes and implications for genetic chemotherapy.
Structure, 11:961-972, 2003

PubMed Abstract: 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.

PubMed: 12906827
DOI: 10.1016/S0969-2126(03)00153-9

Experimental method

X-RAY DIFFRACTION (1.43 Å)