4U9V

Crystal structure of NatD (Naa40p) bound to acetyl CoA

4U9V の概要

• エントリーDOI: 10.2210/pdb4u9v/pdb
• 関連するPDBエントリー: 4U9W 4U9X 4UA3
• 分子名称: N-alpha-acetyltransferase 40, ACETYL COENZYME *A (3 entities in total)
• 機能のキーワード: acetyltransferase, gnat fold, n-terminal acetylation, acetyl-coa, transferase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23719.61

構造登録者

Magin, R.S.,Liszczak, G.P.,Marmorstein, R. (登録日: 2014-08-06, 公開日: 2015-01-28, 最終更新日: 2024-11-06)

主引用文献

Magin, R.S.,Liszczak, G.P.,Marmorstein, R.
The Molecular Basis for Histone H4- and H2A-Specific Amino-Terminal Acetylation by NatD.
Structure, 23:332-341, 2015

PubMed Abstract: N-terminal acetylation is among the most common protein modifications in eukaryotes and is mediated by evolutionarily conserved N-terminal acetyltransferases (NATs). NatD is among the most selective NATs; its only known substrates are histones H4 and H2A, containing the N-terminal sequence SGRGK in humans. Here we characterize the molecular basis for substrate-specific acetylation by NatD by reporting its crystal structure bound to cognate substrates and performing related biochemical studies. A novel N-terminal segment wraps around the catalytic core domain to make stabilizing interactions, and the α1-α2 and β6-β7 loops adopt novel conformations to properly orient the histone N termini in the binding site. Ser1 and Arg3 of the histone make extensive contacts to highly conserved NatD residues in the substrate binding pocket, and flanking glycine residues also appear to contribute to substrate-specific binding by NatD, together defining a Ser-Gly-Arg-Gly recognition sequence. These studies have implications for understanding substrate-specific acetylation by NAT enzymes.

PubMed: 25619998
DOI: 10.1016/j.str.2014.10.025

実験手法

X-RAY DIFFRACTION (1.78 Å)