Crystal Structure of the Golgi-Associated Human Nα-Acetyltransferase 60 Reveals the Molecular Determinants for Substrate-Specific Acetylation
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- 作者：Svein Isungset Stø ; ve1 ; 2 ; Robert S. Magin3 ; 4 ; 5 ; Hå ; vard Foyn1 ; Bengt Erik Haug6 ; Ronen Marmorstein3 ; 4 ; 5 ; marmor@mail.med.upenn.edu" class="auth_mail" title="E-mail the corresponding author ; Thomas Arnesen1 ; 2 ; thomas.arnesen@uib.no" class="auth_mail" title="E-mail the corresponding author
- 关键词：acetyltransferase ; crystal structure ; Naa60 ; NAT ; NatF ; N-terminal acetylation
- 刊名：Structure
- 出版年：2016
- 出版时间：6 July 2016
- 年：2016
- 卷：24
- 期：7
- 页码：1044-1056
- 全文大小：4616 K
文摘
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Crystal structure of Naa60, a unique membrane-associated N-terminal acetyltransferase
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Naa60-specific loops are important for enzyme stability and substrate binding
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20">Naa60 β6-β7 loop mediates dimer to monomer transition for substrate-specific binding
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25">A novel CoA-peptide bisubstrate Naa60-inhibitor was developed and co-crystallized