1. Structural insights to heterodimeric cis-prenyltransferases through yeast dehydrodolichyl diphosphate synthase subunit Nus1.
- Author
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Ma, Jiantao, Ko, Tzu-Ping, Yu, Xuejing, Zhang, Lilan, Ma, Lixin, Zhai, Chao, Guo, Rey-Ting, Liu, Weidong, Li, HuaZhong, and Chen, Chun-Chi
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HETERODIMERS , *YEAST , *SACCHAROMYCES cerevisiae , *CRYSTAL structure , *HOMODIMERS , *X-ray crystallography - Abstract
The polyprenoid glycan carriers are produced by cis -prenyltransferases (cis -PTs), which function as heterodimers in metazoa and fungi or homodimers in bacteria, but both are found in plants, protista and archaea. Heterodimeric cis -PTs comprise catalytic and non-catalytic subunits while homodimeric enzymes contain two catalytic subunits. The non-catalytic subunits of cis -PT shows low sequence similarity to known cis -PTs and their structure information is of great interests. Here we report the crystal structure of Nus1, the non-catalytic subunit of cis -PT from Saccharomyces cerevisiae. We also investigate the heterodimer formation and active site conformation by constructing a homology model of Nus1 and its catalytic subunit. Nus1 does not contain an active site, but its C-terminus may participate in catalysis by interacting with the substrates bound to the catalytic subunit. These results provide important basis for further investigation of heterodimeric cis -PTs. • The structure of N-terminally truncated Nus1 was determined at 2.0 Å resolution. • Significant differences from other cis -prenyltransferase structures were observed. • A model of Nus1/Rer2 complex suggests conserved subunit interface and active site. • The C-terminus of Nus1 interacts with Rer2 but does not contain an RXG motif. • A majority of disease-causing mutation sites in human NgBR can now be located. [ABSTRACT FROM AUTHOR]
- Published
- 2019
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