2j5c
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RATIONAL CONVERSION OF SUBSTRATE AND PRODUCT SPECIFICITY IN A MONOTERPENE SYNTHASE. STRUCTURAL INSIGHTS INTO THE MOLECULAR BASIS OF RAPID EVOLUTION.
OverviewOverview
Terpene synthases are responsible for the biosynthesis of the complex, chemical defense arsenal of plants and microorganisms. How do these, enzymes, which all appear to share a common terpene synthase fold, specify, the many different products made almost entirely from one of only three, substrates? Elucidation of the structure of 1,8-cineole synthase from, Salvia fruticosa (Sf-CinS1) combined with analysis of functional and, phylogenetic relationships of enzymes within Salvia species identified, active-site residues responsible for product specificity. Thus, Sf-CinS1, was successfully converted to a sabinene synthase with a minimum number of, rationally predicted substitutions, while identification of the Asn side, chain essential for water activation introduced 1,8-cineole and, ... [(full description)]
About this StructureAbout this Structure
2J5C is a [Single protein] structure of sequence from [Salvia fruticosa] with BME as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Rational Conversion of Substrate and Product Specificity in a Salvia Monoterpene Synthase: Structural Insights into the Evolution of Terpene Synthase Function., Kampranis SC, Ioannidis D, Purvis A, Mahrez W, Ninga E, Katerelos NA, Anssour S, Dunwell JM, Degenhardt J, Makris AM, Goodenough PW, Johnson CB, Plant Cell. 2007 Jun 8;. PMID:17557809
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