1DI1

CRYSTAL STRUCTURE OF ARISTOLOCHENE SYNTHASE FROM PENICILLIUM ROQUEFORTI

Summary for 1DI1

• Entry DOI: 10.2210/pdb1di1/pdb
• Related: 1DGP 1F1K 1F1L 1F1N 1F1P
• Descriptor: ARISTOLOCHENE SYNTHASE (2 entities in total)
• Functional Keywords: sesquiterpene cyclase, isoprenoid biosynthesis, lyase
• Biological source: Penicillium roqueforti
• Total number of polymer chains: 2
• Total formula weight: 68994.42

Authors

Caruthers, J.M.,Kang, I.,Cane, D.E.,Christianson, D.W.,Rynkiewicz, M.J. (deposition date: 1999-11-28, release date: 2000-08-30, Last modification date: 2024-02-07)

Primary citation

Caruthers, J.M.,Kang, I.,Rynkiewicz, M.J.,Cane, D.E.,Christianson, D.W.
Crystal structure determination of aristolochene synthase from the blue cheese mold, Penicillium roqueforti.
J.Biol.Chem., 275:25533-25539, 2000

PubMed Abstract: 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.

PubMed: 10825154
DOI: 10.1074/jbc.M000433200

Experimental method

X-RAY DIFFRACTION (2.5 Å)