4LX9

Archaeal amino-terminal acetyltransferase (NAT) bound to acetyl coenzyme A

4LX9 の概要

• エントリーDOI: 10.2210/pdb4lx9/pdb
• 関連するPDBエントリー: 2X7B 3TFY 4KVM 4KVO 4KVX
• 分子名称: ARCHAEAL AMINO-TERMINAL ACETYLTRANSFERASE, ACETYL COENZYME *A, ZINC ION, ... (4 entities in total)
• 機能のキーワード: transferase, amino-terminal acetyltransferase, gnat fold, amino-terminal acetyltransferase (nat)
• 由来する生物種: Sulfolobus solfataricus
• 細胞内の位置: Cytoplasm (Potential): Q980R9
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20413.95

構造登録者

Liszczak, G.P.,Marmorstein, R. (登録日: 2013-07-29, 公開日: 2013-08-21, 最終更新日: 2024-02-28)

主引用文献

Liszczak, G.,Marmorstein, R.
Implications for the evolution of eukaryotic amino-terminal acetyltransferase (NAT) enzymes from the structure of an archaeal ortholog.
Proc.Natl.Acad.Sci.USA, 110:14652-14657, 2013

PubMed Abstract: Amino-terminal acetylation is a ubiquitous modification in eukaryotes that is involved in a growing number of biological processes. There are six known eukaryotic amino-terminal acetyltransferases (NATs), which are differentiated from one another on the basis of substrate specificity. To date, two eukaryotic NATs, NatA and NatE, have been structurally characterized, of which NatA will acetylate the α-amino group of a number of nonmethionine amino-terminal residue substrates such as serine; NatE requires a substrate amino-terminal methionine residue for activity. Interestingly, these two NATs use different catalytic strategies to accomplish substrate-specific acetylation. In archaea, where this modification is less prevalent, only one NAT enzyme has been identified. Surprisingly, this enzyme is able to acetylate NatA and NatE substrates and is believed to represent an ancestral NAT variant from which the eukaryotic NAT machinery evolved. To gain insight into the evolution of NAT enzymes, we determined the X-ray crystal structure of an archaeal NAT from Sulfolobus solfataricus (ssNAT). Through the use of mutagenesis and kinetic analysis, we show that the active site of ssNAT represents a hybrid of the NatA and NatE active sites, and we highlight features of this protein that allow it to facilitate catalysis of distinct substrates through different catalytic strategies, which is a unique characteristic of this enzyme. Taken together, the structural and biochemical data presented here have implications for the evolution of eukaryotic NAT enzymes and the substrate specificities therein.

PubMed: 23959863
DOI: 10.1073/pnas.1310365110

実験手法

X-RAY DIFFRACTION (1.98 Å)