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-Structure paper
タイトル | Structural insight on assembly-line catalysis in terpene biosynthesis. |
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ジャーナル・号・ページ | Nat Commun, Vol. 12, Issue 1, Page 3487, Year 2021 |
掲載日 | 2021年6月9日 |
著者 | Jacque L Faylo / Trevor van Eeuwen / Hee Jong Kim / Jose J Gorbea Colón / Benjamin A Garcia / Kenji Murakami / David W Christianson / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:34108468 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 4.0 - 11.9 Å |
構造データ | EMDB-22473, PDB-7jth: EMDB-22484: EMDB-22485: EMDB-22487: EMDB-22488: EMDB-22489: EMDB-23602: EMDB-23610: EMDB-23611: |
由来 |
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キーワード | TRANSFERASE / LYASE / GGPP Synthase / Prenyltransferase |