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TitleStructure and mechanism of a eukaryotic ceramide synthase complex.
Journal, issue, pagesEMBO J, Vol. 42, Issue 24, Page e114889, Year 2023
Publish dateDec 11, 2023
AuthorsTian Xie / Qi Fang / Zike Zhang / Yanfei Wang / Feitong Dong / Xin Gong /
PubMed AbstractCeramide synthases (CerS) catalyze ceramide formation via N-acylation of a sphingoid base with a fatty acyl-CoA and are attractive drug targets for treating numerous metabolic diseases and cancers. ...Ceramide synthases (CerS) catalyze ceramide formation via N-acylation of a sphingoid base with a fatty acyl-CoA and are attractive drug targets for treating numerous metabolic diseases and cancers. Here, we present the cryo-EM structure of a yeast CerS complex, consisting of a catalytic Lac1 subunit and a regulatory Lip1 subunit, in complex with C26-CoA substrate. The CerS holoenzyme exists as a dimer of Lac1-Lip1 heterodimers. Lac1 contains a hydrophilic reaction chamber and a hydrophobic tunnel for binding the CoA moiety and C26-acyl chain of C26-CoA, respectively. Lip1 interacts with both the transmembrane region and the last luminal loop of Lac1 to maintain the proper acyl chain binding tunnel. A lateral opening on Lac1 serves as a potential entrance for the sphingoid base substrate. Our findings provide a template for understanding the working mechanism of eukaryotic ceramide synthases and may facilitate the development of therapeutic CerS modulators.
External linksEMBO J / PubMed:37953642 / PubMed Central
MethodsEM (single particle)
Resolution3.09 - 3.85 Å
Structure data

35862

8izd

EMDB-35862, PDB-8izd:
Cryo-EM structure of the C26-CoA-bound Lac1-Lip1 complex
Method: EM (single particle) / Resolution: 3.09 Å

35863

8izf

EMDB-35863, PDB-8izf:
Cryo-EM structure of the Lac1-Lip1 (Lip1-S74F) complex
Method: EM (single particle) / Resolution: 3.85 Å

Chemicals

ChemComp-6PL:
(4S,7R)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSAN-1-AMINIUM 4-OXIDE / phospholipid*YM

ChemComp-9NY:
Hexacosanoyl-CoA

Source
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
KeywordsTRANSFERASE / Substrate / Complex

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