1n23 | pdb_00001n23

(+)-Bornyl diphosphate synthase: Complex with Mg, pyrophosphate, and (1R,4S)-2-azabornane

spinqualitylabelsall models 1n23, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1n23 is a 2 chain structure with sequence from Salof. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 2BN, MG, POP Related: 1n1b, 1n1z, 1n20, 1n21, 1n22, 1n24 Activity: (+)-bornyl diphosphate synthase, with EC number 5.5.1.8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [BPPS_SALOF] Catalyzes the formation of the (+)-camphor precursor (+)-bornyl diphosphate from geranyl diphosphate. The enzyme also produces significant amounts of (+)-alpha-pinene, (+)-camphene, and (+-)-limonene. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Bornyl diphosphate synthase: structure and strategy for carbocation manipulation by a terpenoid cyclase.,Whittington DA, Wise ML, Urbansky M, Coates RM, Croteau RB, Christianson DW Proc Natl Acad Sci U S A. 2002 Nov 26;99(24):15375-80. Epub 2002 Nov 13. PMID:12432096 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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