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1N24

(+)-Bornyl diphosphate synthase: Complex with Mg and product

Summary for 1N24
Entry DOI10.2210/pdb1n24/pdb
Related1N1B 1N1Z 1N20 1N21 1N22 1N23
Descriptor(+)-bornyl diphosphate synthase, MAGNESIUM ION, (+)-BORNYL DIPHOSPHATE, ... (4 entities in total)
Functional Keywordsterpene synthase fold, isomerase
Biological sourceSalvia officinalis (garden sage)
Cellular locationPlastid, chloroplast: O81192
Total number of polymer chains2
Total formula weight128839.53
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 citationWhittington, 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 cyclase
Proc.Natl.Acad.Sci.USA, 99:15375-15380, 2002
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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