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TitleElectron cryomicroscopy observation of acyl carrier protein translocation in type I fungal fatty acid synthase.
Journal, issue, pagesSci Rep, Vol. 9, Issue 1, Page 12987, Year 2019
Publish dateSep 10, 2019
AuthorsJennifer W Lou / Kali R Iyer / S M Naimul Hasan / Leah E Cowen / Mohammad T Mazhab-Jafari /
PubMed AbstractDuring fatty acid biosynthesis, acyl carrier proteins (ACPs) from type I fungal fatty acid synthase (FAS) shuttle substrates and intermediates within a reaction chamber that hosts multiple spatially- ...During fatty acid biosynthesis, acyl carrier proteins (ACPs) from type I fungal fatty acid synthase (FAS) shuttle substrates and intermediates within a reaction chamber that hosts multiple spatially-fixed catalytic centers. A major challenge in understanding the mechanism of ACP-mediated substrate shuttling is experimental observation of its transient interaction landscape within the reaction chamber. Here, we have shown that ACP spatial distribution is sensitive to the presence of substrates in a catalytically inhibited state, which enables high-resolution investigation of the ACP-dependent conformational transitions within the enoyl reductase (ER) reaction site. In two fungal FASs with distinct ACP localization, the shuttling domain is targeted to the ketoacyl-synthase (KS) domain and away from other catalytic centers, such as acetyl-transferase (AT) and ER domains by steric blockage of the KS active site followed by addition of substrates. These studies strongly suggest that acylation of phosphopantetheine arm of ACP may be an integral part of the substrate shuttling mechanism in type I fungal FAS.
External linksSci Rep / PubMed:31506493 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 3.3 Å
Structure data

20655

6u5t

EMDB-20655, PDB-6u5t:
Electron cryomicroscopy Structure of S. cerevisiae FAS in the Apo state
Method: EM (single particle) / Resolution: 2.9 Å

20656

6u5u

EMDB-20656, PDB-6u5u:
Electron cryomicroscopy Structure of S. cerevisiae FAS in the KS-stalled state
Method: EM (single particle) / Resolution: 2.8 Å

20657

6u5v

EMDB-20657, PDB-6u5v:
Electron cryomicroscopy Structure of C. albicans FAS in the Apo state
Method: EM (single particle) / Resolution: 2.8 Å

20658

6u5w

EMDB-20658, PDB-6u5w:
Electron cryomicroscopy structure of C. albicans FAS in the KS-stalled state
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-PNS:
4'-PHOSPHOPANTETHEINE / Phosphopantetheine

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE / Flavin mononucleotide

ChemComp-NAP:
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / Nicotinamide adenine dinucleotide phosphate

Source
  • saccharomyces cerevisiae (brewer's yeast)
  • Baker's yeast (brewer's yeast)
  • candida albicans (yeast)
  • Yeast (yeast)
KeywordsTRANSFERASE / Fungal Fatty acid synthase

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