Structural elucidation of the cis -prenyltransferase NgBR/DHDDS complex reveals insights in regulation of protein glycosylation | Zendy

Ban H. Edani | Zendy; Kariona A. Grabińska | Zendy; Rong Zhang | Zendy; Eon Joo Park | Zendy; Benjamin Siciliano | Zendy; Liliana Surmacz | Zendy; Ya Ha | Zendy; William C. Sessa | Zendy

Open Access

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

Author(s) -

Ban H. Edani,

Kariona A. Grabińska,

Rong Zhang,

Eon Joo Park,

Benjamin Siciliano,

Liliana Surmacz,

Ya Ha,

William C. Sessa

Publication year - 2020

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.2008381117

Subject(s) - prenyltransferase , glycosylation , enzyme , biology , chemistry , microbiology and biotechnology , biochemistry , prenylation

Significance The enzyme,cis- prenyltransferase (cis- PTase), composed of two subunits, NgBR and DHDDS, is essential for protein glycosylation reactions in all higher eukaryotes. Here, we report the heterodimeric crystal structure of the complex and show features that impacts the stability, activity, and lipid sensing of enzyme complex. Moreover, the structure rationalizes mutations that cause genetic disorders of glycosylation leading to cognitive dysfunction, epilepsy, and Parkinson’s disease.

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