1jfg
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(New page: 200px<br /><applet load="1jfg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jfg, resolution 2.5Å" /> '''TRICHODIENE SYNTHASE ...)
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Revision as of 16:04, 20 November 2007
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TRICHODIENE SYNTHASE FROM FUSARIUM SPOROTRICHIOIDES COMPLEXED WITH DIPHOSPHATE
Overview
The x-ray crystal structure of recombinant trichodiene synthase from, Fusarium sporotrichioides has been determined to 2.5-A resolution, both, unliganded and complexed with inorganic pyrophosphate. This reaction, product coordinates to three Mg(2+) ions near the mouth of the active site, cleft. A comparison of the liganded and unliganded structures reveals a, ligand-induced conformational change that closes the mouth of the active, site cleft. Binding of the substrate farnesyl diphosphate similarly may, trigger this conformational change, which would facilitate catalysis by, protecting reactive carbocationic intermediates in the cyclization, cascade. Trichodiene synthase also shares significant structural, similarity with other sesquiterpene synthases despite a lack of, significant sequence identity. This similarity indicates divergence from a, common ancestor early in the evolution of terpene biosynthesis.
About this Structure
1JFG is a Single protein structure of sequence from Fusarium sporotrichioides with MG, POP and GOL as ligands. Active as Trichodiene synthase, with EC number 4.2.3.6 Full crystallographic information is available from OCA.
Reference
Structure of trichodiene synthase from Fusarium sporotrichioides provides mechanistic inferences on the terpene cyclization cascade., Rynkiewicz MJ, Cane DE, Christianson DW, Proc Natl Acad Sci U S A. 2001 Nov 20;98(24):13543-8. Epub 2001 Nov 6. PMID:11698643
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