1f1p | pdb_00001f1p

THEORETICAL MODEL OF ARISTOLOCHENE SYNTHASE COMPLEXED WITH ITS SUBSTRATE, FARNESYL DIPHOSPHATE

spinqualitylabelsall models 1f1p Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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