1N21

(+)-Bornyl Diphosphate Synthase: Cocrystal with Mg and 3-aza-2,3-dihydrogeranyl diphosphate

Summary for 1N21

• Entry DOI: 10.2210/pdb1n21/pdb
• Related: 1N1B 1N1Z 1N20 1N22 1N23 1N24
• Descriptor: (+)-bornyl diphosphate synthase, MAGNESIUM ION, 2-[METHYL-(4-METHYL-PENT-3-ENYL)-AMINO]-ETHYL-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: terpene synthase fold, isomerase
• Biological source: Salvia officinalis (garden sage)
• Cellular location: Plastid, chloroplast: O81192
• Total number of polymer chains: 1
• Total formula weight: 64422.77

Authors

Whittington, D.A.,Wise, M.L.,Urbansky, M.,Coates, R.M.,Croteau, R.B.,Christianson, D.W. (deposition date: 2002-10-21, release date: 2002-11-27, Last modification date: 2024-02-14)

Primary citation

Whittington, D.A.,Wise, M.L.,Urbansky, M.,Coates, R.M.,Croteau, R.B.,Christianson, D.W.
Bornyl diphosphate synthase: Structure and strategy for carbocation manipulation by a terpenoid synthase
Proc.Natl.Acad.Sci.USA, 99:15375-15380, 2002

PubMed 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.

PubMed: 12432096
DOI: 10.1073/pnas.232591099

Experimental method

X-RAY DIFFRACTION (3.1 Å)