Structural elucidation of the <i>cis</i>-prenyltransferase NgBR/DHDDS complex reveals insights in regulation of protein glycosylation.

ABSTRACT: Cis-prenyltransferase (cis-PTase) catalyzes the rate-limiting step in the synthesis of glycosyl carrier lipids required for protein glycosylation in the lumen of endoplasmic reticulum. Here, we report the crystal structure of the human NgBR/DHDDS complex, which represents an atomic resolution structure for any heterodimeric cis-PTase. The crystal structure sheds light on how NgBR stabilizes DHDDS through dimerization, participates in the enzyme's active site through its C-terminal -RXG- motif, and how phospholipids markedly stimulate cis-PTase activity. Comparison of NgBR/DHDDS with homodimeric cis-PTase structures leads to a model where the elongating isoprene chain extends beyond the enzyme's active site tunnel, and an insert within the α3 helix helps t

SUBMITTER: Edani BH 

PROVIDER: S-EPMC7456142 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature