9NNQ

GNAT family acetyltransferase EryM

9NNQ の概要

• エントリーDOI: 10.2210/pdb9nnq/pdb
• 分子名称: Lysine N-acyltransferase MbtK, MAGNESIUM ION, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: gnat, acetyltransferase, erythrochelin, transferase
• 由来する生物種: Saccharopolyspora erythraea
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 96749.39

構造登録者

Li, Y.,Smith, J. (登録日: 2025-03-06, 公開日: 2025-05-28, 最終更新日: 2025-08-20)

主引用文献

Li, Y.,Liu, X.,Harris, N.R.,Roberts, J.R.,Valdivia, E.M.,Ji, X.,Smith, J.L.
Redefining the role of the EryM acetyltransferase in natural product biosynthetic pathways.
Structure, 33:1352-1361.e3, 2025

PubMed Abstract: The GNAT (GCN5-related N-acetyltransferase) superfamily comprises enzymes with a conserved fold and diverse catalytic activities, including primarily acyl transfer, with a few examples of decarboxylation. EryM, a GNAT from Saccharopolyspora erythraea, has been implicated in both erythromycin and erythrochelin biosynthesis, with dual functionality as an acetyltransferase and a decarboxylase. Despite an historical association with malonyl-coenzyme A decarboxylation activity, this dual activity has remained enigmatic as its close homologs were identified with only acyl transfer activity. Here, functional assays demonstrate that EryM catalyzes acyl transfer but lacks decarboxylation activity, challenging long-standing assumptions about its biosynthetic role. Crystal structures of EryM and an acetyl-CoA complex and comparison with homologs in siderophore pathways reveal a conserved catalytic pocket with an essential His and identically positioned side chains common to GNAT enzymes for N-acyl transfer from CoA to primary hydroxylamine substrates. Bioinformatic analysis defines a large GNAT subfamily broadly distributed in the microbial world.

PubMed: 40516533
DOI: 10.1016/j.str.2025.05.011

実験手法

X-RAY DIFFRACTION (2.5 Å)