Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 104, Issue 13, Pages 5360-5365Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0700915104
Keywords
crystal structure; geranyl diphosphate; linalyl diphosphate; monoterpene cyclase; monoterpene synthase
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Funding
- NIGMS NIH HHS [GM13956, R01 GM013956, GM31354, R37 GM031354] Funding Source: Medline
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The crystal structure of (4S)-limonene synthase from Meniha spicata, a metal ion-dependent monoterpene cyclase that catalyzes the coupled isomerization and cyclization of geranyl diphosphate, is reported at 2.7-angstrom resolution in two forms liganded to the substrate and intermediate analogs, 2-fluorogeranyl diphosphate and 2-fluorolinalyl diphosphate, respectively. The implications of these findings are described for domain interactions in the homodimer and for changes in diphosphate-metal ion coordination and substrate binding conformation in the course of the multistep reaction.
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