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Bornyl diphosphate synthase: structure and strategy for carbocation manipulation by a terpenoid cyclase.

ABSTRACT: The x-ray crystal structure of dimeric (+)-bornyl diphosphate synthase, a metal-requiring monoterpene cyclase from Salvia officinalis, is reported at 2.0-A resolution. Each monomer contains two alpha-helical domains: the C-terminal domain catalyzes the cyclization of geranyl diphosphate, orienting and stabilizing multiple reactive carbocation intermediates; the N-terminal domain has no clearly defined function, although its N terminus caps the active site in the C-terminal domain during catalysis. Structures of complexes with aza analogues of substrate and carbocation intermediates, as well as complexes with pyrophosphate and bornyl diphosphate, provide "snapshots" of the terpene cyclization cascade.

SUBMITTER: Whittington DA

PROVIDER: S-EPMC137724 | biostudies-literature | 2002 Nov

REPOSITORIES: biostudies-literature

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Bornyl diphosphate synthase: structure and strategy for carbocation manipulation by a terpenoid cyclase.

Whittington Douglas A DA Wise Mitchell L ML Urbansky Marek M Coates Robert M RM Croteau Rodney B RB Christianson David W DW

Proceedings of the National Academy of Sciences of the United States of America 20021113 24

The x-ray crystal structure of dimeric (+)-bornyl diphosphate synthase, a metal-requiring monoterpene cyclase from Salvia officinalis, is reported at 2.0-A resolution. Each monomer contains two alpha-helical domains: the C-terminal domain catalyzes the cyclization of geranyl diphosphate, orienting and stabilizing multiple reactive carbocation intermediates; the N-terminal domain has no clearly defined function, although its N terminus caps the active site in the C-terminal domain during catalysi ...[more]

PMID: 12432096

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