1n1b
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(New page: 200px<br /><applet load="1n1b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n1b, resolution 2.00Å" /> '''Crystal Structure of...)
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Revision as of 19:44, 20 November 2007
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Crystal Structure of (+)-Bornyl Diphosphate Synthase from Sage
Overview
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.
About this Structure
1N1B is a Single protein structure of sequence from Salvia officinalis with MG and HG as ligands. Active as Geranyl-diphosphate cyclase, with EC number 5.5.1.8 Full crystallographic information is available from OCA.
Reference
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
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