Structures of DPAGT1 Explain Glycosylation Disease Mechanisms and Advance TB Antibiotic Design.

doi:10.1016/j.cell.2018.10.037

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Article

Structures of DPAGT1 Explain Glycosylation Disease Mechanisms and Advance TB Antibiotic Design.

Cell - 1 Nov 2018

Dong Yin Yao, Wang Hua, Pike Ashley C W, Cochrane Stephen A, Hamedzadeh Sadra, Wyszyński Filip J, Bushell Simon R, Royer Sylvain F, Widdick David A, Sajid Andaleeb, Boshoff Helena I, Park Yumi, Lucas Ricardo, Liu Wei-Min, Lee Seung Seo, Machida Takuya, Minall Leanne, Mehmood Shahid, Belaya Katsiaryna, Liu Wei-Wei, Chu Amy, Shrestha Leela, Mukhopadhyay Shubhashish M M, Strain-Damerell Claire, Chalk Rod, Burgess-Brown Nicola A, Bibb Mervyn J, Barry Iii Clifton E, Robinson Carol V, Beeson David, Davis Benjamin G, Carpenter Elisabeth P

Abstract excerpt

Protein N-glycosylation is a widespread post-translational modification. The first committed step in this process is catalysed by dolichyl-phosphate N-acetylglucosamine-phosphotransferase DPAGT1 (GPT/E.C. 2.7.8.15). Missense DPAGT1 variants cause congenital myasthenic syndrome and disorders of glycosylation. In addition, naturally-occurring bactericidal nucleoside analogues such as tunicamycin are toxic to...

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Identifiers

PMID: 30388443
DOI: 10.1016/j.cell.2018.10.037
PMCID: PMC6218659

Genes

DPAGT1
GPT

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