3LNB

Crystal Structure Analysis of Arylamine N-acetyltransferase C from Bacillus anthracis

3LNB の概要

• エントリーDOI: 10.2210/pdb3lnb/pdb
• 分子名称: N-acetyltransferase family protein, COENZYME A, FORMIC ACID, ... (4 entities in total)
• 機能のキーワード: arylamine n-acetyltransferase, transferase, nat, acetyltransferase, acyltransferase
• 由来する生物種: Bacillus anthracis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36162.07

構造登録者

Li de la Sierra-Gallay, I.,Pluvinage, B.,Rodrigues-Lima, F. (登録日: 2010-02-02, 公開日: 2011-01-26, 最終更新日: 2023-11-01)

主引用文献

Pluvinage, B.,Li de la Sierra-Gallay, I.,Kubiak, X.,Xu, X.,Dairou, J.,Dupret, J.M.,Rodrigues-Lima, F.
The Bacillus anthracis arylamine N-acetyltransferase ((BACAN)NAT1) that inactivates sulfamethoxazole, reveals unusual structural features compared with the other NAT isoenzymes.
Febs Lett., 585:3947-3952, 2011

PubMed Abstract: Arylamine N-acetyltransferases (NATs) are xenobiotic-metabolizing enzymes that biotransform arylamine drugs. The Bacillus anthracis (BACAN)NAT1 enzyme affords increased resistance to the antibiotic sulfamethoxazole through its acetylation. We report the structure of (BACAN)NAT1. Unexpectedly, endogenous coenzymeA was present in the active site. The structure suggests that, contrary to the other prokaryotic NATs, (BACAN)NAT1 possesses a 14-residue insertion equivalent to the "mammalian insertion", a structural feature considered unique to mammalian NATs. Moreover, (BACAN)NAT1 structure shows marked differences in the mode of binding and location of coenzymeA when compared to the other NATs. This suggests that the mechanisms of cofactor recognition by NATs is more diverse than expected and supports the cofactor-binding site as being a unique subsite to target in drug design against bacterial NATs.

PubMed: 22062153
DOI: 10.1016/j.febslet.2011.10.041

実験手法

X-RAY DIFFRACTION (2.01 Å)