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 2.5&Aring;" /> '''TRICHODIENE SYNTHASE ...)
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[[Image:1jfg.jpg|left|200px]]<br /><applet load="1jfg" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1jfg, resolution 2.5&Aring;" />
caption="1jfg, resolution 2.5&Aring;" />
'''TRICHODIENE SYNTHASE FROM FUSARIUM SPOROTRICHIOIDES COMPLEXED WITH DIPHOSPHATE'''<br />
'''TRICHODIENE SYNTHASE FROM FUSARIUM SPOROTRICHIOIDES COMPLEXED WITH DIPHOSPHATE'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1JFG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_sporotrichioides Fusarium sporotrichioides] with MG, POP and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Trichodiene_synthase Trichodiene synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.6 4.2.3.6] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JFG OCA].
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1JFG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_sporotrichioides Fusarium sporotrichioides] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=POP:'>POP</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Trichodiene_synthase Trichodiene synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.6 4.2.3.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JFG OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Trichodiene synthase]]
[[Category: Trichodiene synthase]]
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[[Category: Cane, D.E.]]
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[[Category: Cane, D E.]]
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[[Category: Christianson, D.W.]]
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[[Category: Christianson, D W.]]
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[[Category: Rynkiewicz, M.J.]]
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[[Category: Rynkiewicz, M J.]]
[[Category: GOL]]
[[Category: GOL]]
[[Category: MG]]
[[Category: MG]]
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[[Category: terpenoid synthase fold]]
[[Category: terpenoid synthase fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:11:47 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:22:03 2008''

Revision as of 11:22, 21 February 2008


1jfg, resolution 2.5Å

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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 , and 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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