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TitleStructural insight on assembly-line catalysis in terpene biosynthesis.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 3487, Year 2021
Publish dateJun 9, 2021
AuthorsJacque L Faylo / Trevor van Eeuwen / Hee Jong Kim / Jose J Gorbea Colón / Benjamin A Garcia / Kenji Murakami / David W Christianson /
PubMed AbstractFusicoccadiene synthase from Phomopsis amygdali (PaFS) is a unique bifunctional terpenoid synthase that catalyzes the first two steps in the biosynthesis of the diterpene glycoside Fusicoccin A, a ...Fusicoccadiene synthase from Phomopsis amygdali (PaFS) is a unique bifunctional terpenoid synthase that catalyzes the first two steps in the biosynthesis of the diterpene glycoside Fusicoccin A, a mediator of 14-3-3 protein interactions. The prenyltransferase domain of PaFS generates geranylgeranyl diphosphate, which the cyclase domain then utilizes to generate fusicoccadiene, the tricyclic hydrocarbon skeleton of Fusicoccin A. Here, we use cryo-electron microscopy to show that the structure of full-length PaFS consists of a central octameric core of prenyltransferase domains, with the eight cyclase domains radiating outward via flexible linker segments in variable splayed-out positions. Cryo-electron microscopy and chemical crosslinking experiments additionally show that compact conformations can be achieved in which cyclase domains are more closely associated with the prenyltransferase core. This structural analysis provides a framework for understanding substrate channeling, since most of the geranylgeranyl diphosphate generated by the prenyltransferase domains remains on the enzyme for cyclization to form fusicoccadiene.
External linksNat Commun / PubMed:34108468 / PubMed Central
MethodsEM (single particle)
Resolution4.0 - 11.9 Å
Structure data

22473

7jth

EMDB-22473, PDB-7jth:
Cryo-EM structure of unliganded octameric prenyltransferase domain of Phomopsis amygdali fusicoccadiene synthase
Method: EM (single particle) / Resolution: 4.0 Å

EMDB-22484:
Cryo-EM maps of fixed PaFS, an octamer of prenyltransferase domains with transiently interacting cyclase domains in variable positions
Method: EM (single particle) / Resolution: 7.4 Å

EMDB-22485:
Cryo-EM structure of Grafix-stabilized PaFS prenyltransferase octamer with a peripheral cyclase domain - symmetry expanded class A
Method: EM (single particle) / Resolution: 8.5 Å

EMDB-22487:
Cryo-EM structure of Grafix-stabilized PaFS prenyltransferase octamer with a peripheral cyclase domain - symmetry expanded class B
Method: EM (single particle) / Resolution: 8.6 Å

EMDB-22488:
Cryo-EM structure of Grafix-stabilized PaFS prenyltransferase octamer with a peripheral cyclase domain - symmetry expanded class C
Method: EM (single particle) / Resolution: 9.4 Å

EMDB-22489:
Cryo-EM structure of Grafix-stabilized PaFS prenyltransferase octamer with cyclase domain capping octameric central pore
Method: EM (single particle) / Resolution: 11.9 Å

EMDB-23602:
Cryo-EM structure of unliganded octameric prenyltransferase domain of Phomopsis amygdali fusicoccadiene synthase, reconstruction in C1
Method: EM (single particle) / Resolution: 4.18 Å

EMDB-23610:
Cryo-EM asymmetric structure of Grafix-stabilized PaFS octameric prenyltransferase domain
Method: EM (single particle) / Resolution: 7.8 Å

EMDB-23611:
Cryo-EM reconstruction of Grafix-stabilized PaFS octameric prenyltransferase domain
Method: EM (single particle) / Resolution: 7.4 Å

Source
  • phomopsis amygdali (fungus)
  • Diaporthe amygdali (fungus)
KeywordsTRANSFERASE / LYASE / GGPP Synthase / Prenyltransferase

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