1di1 | pdb_00001di1
CRYSTAL STRUCTURE OF ARISTOLOCHENE SYNTHASE FROM PENICILLIUM ROQUEFORTI
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| 1di1, resolution 2.5Å | |||||||||||||
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| Activity: | Aristolochene synthase, with EC number 4.2.3.9 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
1DI1 is a Single protein structure of sequence from Penicillium roqueforti. 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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