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Structure paper

TitleStructural basis of the acyl-transfer mechanism of human GPAT1.
Journal, issue, pagesNat Struct Mol Biol, Vol. 30, Issue 1, Page 22-30, Year 2023
Publish dateDec 15, 2022
AuthorsZachary Lee Johnson / Mark Ammirati / David Jonathan Wasilko / Jeanne S Chang / Stephen Noell / Timothy L Foley / Hyejin Yoon / Kathleen Smith / Shoh Asano / Katherine Hales / Min Wan / Qingyi Yang / Mary A Piotrowski / Kathleen A Farley / Tamara Gilbert / Lisa M Aschenbrenner / Kimberly F Fennell / Jason K Dutra / Mary Xu / Chunyang Guo / Alison E Varghese / Justin Bellenger / Alandra Quinn / Christopher W Am Ende / Graham M West / Matthew C Griffor / Donald Bennett / Matthew Calabrese / Claire M Steppan / Seungil Han / Huixian Wu /
PubMed AbstractGlycerol-3-phosphate acyltransferase (GPAT)1 is a mitochondrial outer membrane protein that catalyzes the first step of de novo glycerolipid biosynthesis. Hepatic expression of GPAT1 is linked to ...Glycerol-3-phosphate acyltransferase (GPAT)1 is a mitochondrial outer membrane protein that catalyzes the first step of de novo glycerolipid biosynthesis. Hepatic expression of GPAT1 is linked to liver fat accumulation and the severity of nonalcoholic fatty liver diseases. Here we present the cryo-EM structures of human GPAT1 in substrate analog-bound and product-bound states. The structures reveal an N-terminal acyltransferase domain that harbors important catalytic motifs and a tightly associated C-terminal domain that is critical for proper protein folding. Unexpectedly, GPAT1 has no transmembrane regions as previously proposed but instead associates with the membrane via an amphipathic surface patch and an N-terminal loop-helix region that contains a mitochondrial-targeting signal. Combined structural, computational and functional studies uncover a hydrophobic pathway within GPAT1 for lipid trafficking. The results presented herein lay a framework for rational inhibitor development for GPAT1.
External linksNat Struct Mol Biol / PubMed:36522428
MethodsEM (single particle)
Resolution3.4 - 3.67 Å
Structure data

27898

8e4y

EMDB-27898, PDB-8e4y:
Cryo-EM structure of human glycerol-3-phosphate acyltransferase 1 (GPAT1) in complex with 2-oxohexadecyl-CoA
Method: EM (single particle) / Resolution: 3.4 Å

27899

8e50

EMDB-27899, PDB-8e50:
Cryo-EM structure of human glycerol-3-phosphate acyltransferase 1 (GPAT1) in complex with CoA and palmitoyl-LPA
Method: EM (single particle) / Resolution: 3.67 Å

Chemicals

ChemComp-UKL:
[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)oxolan-2-yl]methyl (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-{[3-oxo-3-({2-[(2-oxohexadecyl)sulfanyl]ethyl}amino)propyl]amino}butyl dihydrogen diphosphate (non-preferred name)

ChemComp-NKO:
(2R)-2-hydroxy-3-(phosphonooxy)propyl hexadecanoate

ChemComp-COA:
COENZYME A / Coenzyme A

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / acyltransferase / LPA / monotopic / mitochondrial

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