Structural insight into a novel indole prenyltransferase in hapalindole-type alkaloid biosynthesis

被引:9
|
作者
Wang, Jing [1 ]
Chen, Chun-Chi [1 ]
Yang, Yunyun [2 ]
Liu, Weidong [1 ]
Ko, Tzu-Ping [3 ]
Shang, Na [1 ]
Hu, Xiangying [1 ,4 ]
Xie, Yonghua [2 ]
Huang, Jian-Wen [1 ]
Zhang, Yonghui [2 ]
Guo, Rey-Ting [1 ]
机构
[1] Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Tianjin 300308, Peoples R China
[2] Tsinghua Univ, Sch Pharmaceut Sci, Beijing 100084, Peoples R China
[3] Acad Sinica, Inst Biol Chem, Taipei 11529, Taiwan
[4] Jiangnan Univ, Sch Biotechnol, Wuxi 214122, Peoples R China
基金
中国国家自然科学基金;
关键词
Aromatic prenyltransferase; Stigonematales; FamD1; Crystal structure; BIOGENESIS; AMBIGUINE; IDENTIFICATION; FISCHERINDOLE; DISCOVERY; SYSTEM; FAMILY; SUITE;
D O I
10.1016/j.bbrc.2017.12.039
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
FamD1 is a novel CloQfflphB-family indole prenyltransferase which involves in hapalindole-type alkaloid biosynthesis. Here the native FamD1 structure and three protein-ligand complexes are analyzed to investigate the molecular basis of substrate binding and catalysis. FamD1 adopts a typical ABBA architecture of aromatic prenyltransferase, in which the substrate-binding chamber is found in the central beta barrel. The indole-containing acceptor substrate is bound adjacent to the prenyl donor. Based on the complex structures, a catalytic mechanism of FamD1 is proposed. Functional implications on the sister enzyme FamD2 are also discussed. (C) 2017 Elsevier Inc. All rights reserved.
引用
收藏
页码:1782 / 1788
页数:7
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