Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 98, Issue 24, Pages 13543-13548Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.231313098
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- NIGMS NIH HHS [GM30301, R01 GM030301, R37 GM030301, GM56838, R01 GM056838] Funding Source: Medline
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The x-ray crystal structure of recombinant trichodiene synthase from Fusarium sporotrichioides has been determined to 2.5-Angstrom resolution, both unliganded and complexed with inorganic pyrophosphate. This reaction product coordinates to three Mg2+ 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.
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