1JFG

TRICHODIENE SYNTHASE FROM FUSARIUM SPOROTRICHIOIDES COMPLEXED WITH DIPHOSPHATE

Summary for 1JFG

• Entry DOI: 10.2210/pdb1jfg/pdb
• Related: 1JFA
• Descriptor: TRICHODIENE SYNTHASE, GLYCEROL, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: terpenoid synthase fold, lyase
• Biological source: Fusarium sporotrichioides
• Total number of polymer chains: 2
• Total formula weight: 88626.36

Authors

Rynkiewicz, M.J.,Cane, D.E.,Christianson, D.W. (deposition date: 2001-06-20, release date: 2001-11-30, Last modification date: 2023-08-16)

Primary citation

Rynkiewicz, M.J.,Cane, D.E.,Christianson, D.W.
Structure of trichodiene synthase from Fusarium sporotrichioides provides mechanistic inferences on the terpene cyclization cascade.
Proc.Natl.Acad.Sci.USA, 98:13543-13548, 2001

PubMed Abstract: The x-ray crystal structure of recombinant trichodiene synthase from Fusarium sporotrichioides has been determined to 2.5-A resolution, both unliganded and complexed with inorganic pyrophosphate. This reaction product coordinates to three Mg(2+) ions near the mouth of the active site cleft. A comparison of the liganded and unliganded structures reveals a ligand-induced conformational change that closes the mouth of the active site cleft. Binding of the substrate farnesyl diphosphate similarly may trigger this conformational change, which would facilitate catalysis by protecting reactive carbocationic intermediates in the cyclization cascade. Trichodiene synthase also shares significant structural similarity with other sesquiterpene synthases despite a lack of significant sequence identity. This similarity indicates divergence from a common ancestor early in the evolution of terpene biosynthesis.

PubMed: 11698643
DOI: 10.1073/pnas.231313098

Experimental method

X-RAY DIFFRACTION (2.5 Å)