1dgp
From Proteopedia
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ARISTOLOCHENE SYNTHASE FARNESOL COMPLEX
Overview
The 2.5-A resolution crystal structure of recombinant aristolochene, synthase from the blue cheese mold, Penicillium roqueforti, is the first, of a fungal terpenoid cyclase. The structure of the enzyme reveals active, site features that participate in the cyclization of the universal, sesquiterpene cyclase substrate, farnesyl diphosphate, to form the, bicyclic hydrocarbon aristolochene. Metal-triggered carbocation formation, initiates the cyclization cascade, which proceeds through multiple complex, intermediates to yield one exclusive structural and stereochemical isomer, of aristolochene. Structural homology of this fungal cyclase with plant, and bacterial terpenoid cyclases, despite minimal amino acid sequence, identity, suggests divergence from a common, primordial ancestor in the, evolution of terpene biosynthesis.
About this Structure
1DGP is a Single protein structure of sequence from Penicillium roqueforti with FOH as ligand. Active as Aristolochene synthase, with EC number 4.2.3.9 Full crystallographic information is available from OCA.
Reference
Crystal structure determination of aristolochene synthase from the blue cheese mold, Penicillium roqueforti., Caruthers JM, Kang I, Rynkiewicz MJ, Cane DE, Christianson DW, J Biol Chem. 2000 Aug 18;275(33):25533-9. PMID:10825154
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