Dataset Information

Structural basis of heterotetrameric assembly and disease mutations in the human cis-prenyltransferase complex.

ABSTRACT: Strcutural analysis of human cis-prenyltrasnferase showing its architecture in solution as heterotetramer composed of two catalytic dehydrodolichyl diphosphate synthase (DHDDS)units and two inactive Nogo-B receptor (NgBR) units.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Petr Man

LAB HEAD: Petr Man

PROVIDER: PXD021591 | Pride | 2022-02-15

REPOSITORIES: Pride

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Structural basis of heterotetrameric assembly and disease mutations in the human cis-prenyltransferase complex.

Bar-El Michal Lisnyansky ML Vaňková Pavla P Yeheskel Adva A Simhaev Luba L Engel Hamutal H Man Petr P Haitin Yoni Y Giladi Moshe M

Nature communications 20201019 1

The human cis-prenyltransferase (hcis-PT) is an enzymatic complex essential for protein N-glycosylation. Synthesizing the precursor of the glycosyl carrier dolichol-phosphate, mutations in hcis-PT cause severe human diseases. Here, we reveal that hcis-PT exhibits a heterotetrameric assembly in solution, consisting of two catalytic dehydrodolichyl diphosphate synthase (DHDDS) and inactive Nogo-B receptor (NgBR) heterodimers. Importantly, the 2.3 Å crystal structure reveals that the tetramer assem ...[more]

PMID: 33077723

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Dataset Information

Structural basis of heterotetrameric assembly and disease mutations in the human cis-prenyltransferase complex.

Publications

Structural basis of heterotetrameric assembly and disease mutations in the human cis-prenyltransferase complex.

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