1K6W

The Structure of Escherichia coli Cytosine Deaminase

1K6W の概要

• エントリーDOI: 10.2210/pdb1k6w/pdb
• 関連するPDBエントリー: 1k70
• 分子名称: Cytosine Deaminase, FE (III) ION (3 entities in total)
• 機能のキーワード: cytosine deaminase, alpha-beta barrel, hexamer, domain swap, hydrolase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47569.44

構造登録者

Ireton, G.C.,McDermott, G.,Black, M.E.,Stoddard, B.L. (登録日: 2001-10-17, 公開日: 2002-02-06, 最終更新日: 2024-02-07)

主引用文献

Ireton, G.C.,McDermott, G.,Black, M.E.,Stoddard, B.L.
The structure of Escherichia coli cytosine deaminase.
J.Mol.Biol., 315:687-697, 2002

PubMed Abstract: Cytosine deaminase (CD) catalyzes the deamination of cytosine, producing uracil. This enzyme is present in prokaryotes and fungi (but not multicellular eukaryotes) and is an important member of the pyrimidine salvage pathway in those organisms. The same enzyme also catalyzes the conversion of 5-fluorocytosine to 5-fluorouracil; this activity allows the formation of a cytotoxic chemotherapeutic agent from a non-cytotoxic precursor. The enzyme is of widespread interest both for antimicrobial drug design and for gene therapy applications against tumors. The structure of Escherichia coli CD has been determined in the presence and absence of a bound mechanism-based inhibitor. The enzyme forms an (alphabeta)(8) barrel structure with structural similarity to adenosine deaminase, a relationship that is undetectable at the sequence level, and no similarity to bacterial cytidine deaminase. The enzyme is packed into a hexameric assembly stabilized by a unique domain-swapping interaction between enzyme subunits. The active site is located in the mouth of the enzyme barrel and contains a bound iron ion that coordinates a hydroxyl nucleophile. Substrate binding involves a significant conformational change that sequesters the reaction complex from solvent.

PubMed: 11812140
DOI: 10.1006/jmbi.2001.5277

実験手法

X-RAY DIFFRACTION (1.75 Å)