1E2T

Arylamine N-acetyltransferase (NAT) from Salmonella typhimurium

1E2T の概要

• エントリーDOI: 10.2210/pdb1e2t/pdb
• 分子名称: N-HYDROXYARYLAMINE O-ACETYLTRANSFERASE (2 entities in total)
• 機能のキーワード: transferase, acetyl coa dependent
• 由来する生物種: SALMONELLA TYPHIMURIUM
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 260014.82

構造登録者

Sinclair, J.C.,Sandy, J.,Delgoda, R.,Sim, E.,Noble, M.E.M. (登録日: 2000-05-24, 公開日: 2000-07-07, 最終更新日: 2024-05-08)

主引用文献

Sinclair, J.C.,Sandy, J.,Delgoda, R.,Sim, E.,Noble, M.E.M.
Structure of Arylamine N-Acetyltransferase Reveals a Catalytic Triad
Nat.Struct.Biol., 7:560-, 2000

PubMed Abstract: Enzymes of the arylamine N-acetyltransferase (NAT) family are found in species ranging from Escherichia coli to humans. In humans they are known to be responsible for the acetylation of a number of arylamine and hydrazine drugs, and they are strongly linked to the carcinogenic potentiation of certain foreign substances. In prokaryotes their substrate specificities may vary and members of the gene family have been linked to pathways including amide synthesis during rifamycin production. Here we report the crystal structure at 2.8 A resolution of a representative member of this family from Salmonella typhimurium in the presence and absence of a covalently bound product analog. The structure reveals surprising mechanistic information including the presence of a Cys-His-Asp catalytic triad. The fold can be described in terms of three domains of roughly equal length with the second and third domains linked by an interdomain helix. The first two domains, a helical bundle and a beta-barrel, make up the catalytic triad using a structural motif identical to that of the cysteine protease superfamily.

PubMed: 10876241
DOI: 10.1038/76783

実験手法

X-RAY DIFFRACTION (2.8 Å)