1OX7

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

1OX7 の概要

• エントリーDOI: 10.2210/pdb1ox7/pdb
• 分子名称: Cytosine deaminase, ZINC ION, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: aminohydrolase, hydrolase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 36480.70

構造登録者

Ireton, G.C.,Black, M.E.,Stoddard, B.L. (登録日: 2003-04-01, 公開日: 2003-08-19, 最終更新日: 2024-11-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.43 Å)