5HH0

Crystal structure of human Naa60 in complex with CoA

5HH0 の概要

• エントリーDOI: 10.2210/pdb5hh0/pdb
• 関連するPDBエントリー: 5HGZ 5HH1
• 分子名称: N-alpha-acetyltransferase 60, COENZYME A (3 entities in total)
• 機能のキーワード: n-terminal acetylation, nats, protein modification, transferase
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Golgi apparatus membrane : Q9H7X0
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23735.55

構造登録者

Chen, J.Y.,Liu, L.,Yun, C.H. (登録日: 2016-01-09, 公開日: 2016-09-14, 最終更新日: 2023-11-08)

主引用文献

Chen, J.Y.,Liu, L.,Cao, C.L.,Li, M.J.,Tan, K.,Yang, X.,Yun, C.H.
Structure and function of human Naa60 (NatF), a Golgi-localized bi-functional acetyltransferase
Sci Rep, 6:31425-31425, 2016

PubMed Abstract: N-terminal acetylation (Nt-acetylation), carried out by N-terminal acetyltransferases (NATs), is a conserved and primary modification of nascent peptide chains. Naa60 (also named NatF) is a recently identified NAT found only in multicellular eukaryotes. This protein was shown to locate on the Golgi apparatus and mainly catalyze the Nt-acetylation of transmembrane proteins, and it also harbors lysine N(ε)-acetyltransferase (KAT) activity to catalyze the acetylation of lysine ε-amine. Here, we report the crystal structures of human Naa60 (hNaa60) in complex with Acetyl-Coenzyme A (Ac-CoA) or Coenzyme A (CoA). The hNaa60 protein contains an amphipathic helix following its GNAT domain that may contribute to Golgi localization of hNaa60, and the β7-β8 hairpin adopted different conformations in the hNaa60(1-242) and hNaa60(1-199) crystal structures. Remarkably, we found that the side-chain of Phe 34 can influence the position of the coenzyme, indicating a new regulatory mechanism involving enzyme, co-factor and substrates interactions. Moreover, structural comparison and biochemical studies indicated that Tyr 97 and His 138 are key residues for catalytic reaction and that a non-conserved β3-β4 long loop participates in the regulation of hNaa60 activity.

PubMed: 27550639
DOI: 10.1038/srep31425

実験手法

X-RAY DIFFRACTION (1.6 Å)