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http://purl.uniprot.org/citations/19489610http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19489610http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19489610http://www.w3.org/2000/01/rdf-schema#comment"(+)-Delta-cadinene synthase (DCS) from Gossypium arboreum (tree cotton) is a sesquiterpene cyclase that catalyzes the cyclization of farnesyl diphosphate in the first committed step of the biosynthesis of gossypol, a phytoalexin that defends the plant from bacterial and fungal pathogens. Here, we report the X-ray crystal structure of unliganded DCS at 2.4 A resolution and the structure of its complex with three putative Mg(2+) ions and the substrate analogue inhibitor 2-fluorofarnesyl diphosphate (2F-FPP) at 2.75 A resolution. These structures illuminate unusual features that accommodate the trinuclear metal cluster required for substrate binding and catalysis. Like other terpenoid cyclases, DCS contains a characteristic aspartate-rich D(307)DTYD(311) motif on helix D that interacts with Mg(2+)(A) and Mg(2+)(C). However, DCS appears to be unique among terpenoid cyclases in that it does not contain the "NSE/DTE" motif on helix H that specifically chelates Mg(2+)(B), which is usually found as the signature sequence (N,D)D(L,I,V)X(S,T)XXXE (boldface indicates Mg(2+)(B) ligands). Instead, DCS contains a second aspartate-rich motif, D(451)DVAE(455), that interacts with Mg(2+)(B). In this regard, DCS is more similar to the isoprenoid chain elongation enzyme farnesyl diphosphate synthase, which also contains two aspartate-rich motifs, rather than the greater family of terpenoid cyclases. Nevertheless, the structure of the DCS-2F-FPP complex shows that the structure of the trinuclear magnesium cluster is generally similar to that of other terpenoid cyclases despite the alternative Mg(2+)(B) binding motif. Analyses of DCS mutants with alanine substitutions in the D(307)DTYD(311) and D(451)DVAE(455) segments reveal the contributions of these segments to catalysis."xsd:string
http://purl.uniprot.org/citations/19489610http://purl.org/dc/terms/identifier"doi:10.1021/bi900483b"xsd:string
http://purl.uniprot.org/citations/19489610http://purl.org/dc/terms/identifier"doi:10.1021/bi900483b"xsd:string
http://purl.uniprot.org/citations/19489610http://purl.uniprot.org/core/author"Li A."xsd:string
http://purl.uniprot.org/citations/19489610http://purl.uniprot.org/core/author"Li A."xsd:string
http://purl.uniprot.org/citations/19489610http://purl.uniprot.org/core/author"Yu F."xsd:string
http://purl.uniprot.org/citations/19489610http://purl.uniprot.org/core/author"Yu F."xsd:string
http://purl.uniprot.org/citations/19489610http://purl.uniprot.org/core/author"Christianson D.W."xsd:string
http://purl.uniprot.org/citations/19489610http://purl.uniprot.org/core/author"Christianson D.W."xsd:string
http://purl.uniprot.org/citations/19489610http://purl.uniprot.org/core/author"Gennadios H.A."xsd:string
http://purl.uniprot.org/citations/19489610http://purl.uniprot.org/core/author"Gennadios H.A."xsd:string
http://purl.uniprot.org/citations/19489610http://purl.uniprot.org/core/author"Di Costanzo L."xsd:string
http://purl.uniprot.org/citations/19489610http://purl.uniprot.org/core/author"Di Costanzo L."xsd:string
http://purl.uniprot.org/citations/19489610http://purl.uniprot.org/core/author"Gonzalez V."xsd:string
http://purl.uniprot.org/citations/19489610http://purl.uniprot.org/core/author"Gonzalez V."xsd:string
http://purl.uniprot.org/citations/19489610http://purl.uniprot.org/core/author"Miller D.J."xsd:string
http://purl.uniprot.org/citations/19489610http://purl.uniprot.org/core/author"Miller D.J."xsd:string
http://purl.uniprot.org/citations/19489610http://purl.uniprot.org/core/author"Allemann R.K."xsd:string
http://purl.uniprot.org/citations/19489610http://purl.uniprot.org/core/author"Allemann R.K."xsd:string
http://purl.uniprot.org/citations/19489610http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19489610http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19489610http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/19489610http://purl.uniprot.org/core/name"Biochemistry"xsd:string