1dgp

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(New page: 200px<br /><applet load="1dgp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dgp, resolution 2.8&Aring;" /> '''ARISTOLOCHENE SYNTHAS...)
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caption="1dgp, resolution 2.8&Aring;" />
'''ARISTOLOCHENE SYNTHASE FARNESOL COMPLEX'''<br />
'''ARISTOLOCHENE SYNTHASE FARNESOL COMPLEX'''<br />
==Overview==
==Overview==
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The 2.5-A resolution crystal structure of recombinant aristolochene, synthase from the blue cheese mold, Penicillium roqueforti, is the first, of a fungal terpenoid cyclase. The structure of the enzyme reveals active, site features that participate in the cyclization of the universal, sesquiterpene cyclase substrate, farnesyl diphosphate, to form the, bicyclic hydrocarbon aristolochene. Metal-triggered carbocation formation, initiates the cyclization cascade, which proceeds through multiple complex, intermediates to yield one exclusive structural and stereochemical isomer, of aristolochene. Structural homology of this fungal cyclase with plant, and bacterial terpenoid cyclases, despite minimal amino acid sequence, identity, suggests divergence from a common, primordial ancestor in the, evolution of terpene biosynthesis.
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The 2.5-A resolution crystal structure of recombinant aristolochene synthase from the blue cheese mold, Penicillium roqueforti, is the first of a fungal terpenoid cyclase. The structure of the enzyme reveals active site features that participate in the cyclization of the universal sesquiterpene cyclase substrate, farnesyl diphosphate, to form the bicyclic hydrocarbon aristolochene. Metal-triggered carbocation formation initiates the cyclization cascade, which proceeds through multiple complex intermediates to yield one exclusive structural and stereochemical isomer of aristolochene. Structural homology of this fungal cyclase with plant and bacterial terpenoid cyclases, despite minimal amino acid sequence identity, suggests divergence from a common, primordial ancestor in the evolution of terpene biosynthesis.
==About this Structure==
==About this Structure==
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1DGP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Penicillium_roqueforti Penicillium roqueforti] with FOH as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Aristolochene_synthase Aristolochene synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.9 4.2.3.9] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DGP OCA].
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1DGP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Penicillium_roqueforti Penicillium roqueforti] with <scene name='pdbligand=FOH:'>FOH</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Aristolochene_synthase Aristolochene synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.9 4.2.3.9] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DGP OCA].
==Reference==
==Reference==
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[[Category: Penicillium roqueforti]]
[[Category: Penicillium roqueforti]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Cane, D.E.]]
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[[Category: Cane, D E.]]
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[[Category: Caruthers, J.M.]]
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[[Category: Caruthers, J M.]]
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[[Category: Christianson, D.W.]]
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[[Category: Christianson, D W.]]
[[Category: Kang, I.]]
[[Category: Kang, I.]]
[[Category: FOH]]
[[Category: FOH]]
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[[Category: sesquiterpene cyclase]]
[[Category: sesquiterpene cyclase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:16:33 2008''

Revision as of 10:16, 21 February 2008


1dgp, resolution 2.8Å

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ARISTOLOCHENE SYNTHASE FARNESOL COMPLEX

Overview

The 2.5-A resolution crystal structure of recombinant aristolochene synthase from the blue cheese mold, Penicillium roqueforti, is the first of a fungal terpenoid cyclase. The structure of the enzyme reveals active site features that participate in the cyclization of the universal sesquiterpene cyclase substrate, farnesyl diphosphate, to form the bicyclic hydrocarbon aristolochene. Metal-triggered carbocation formation initiates the cyclization cascade, which proceeds through multiple complex intermediates to yield one exclusive structural and stereochemical isomer of aristolochene. Structural homology of this fungal cyclase with plant and bacterial terpenoid cyclases, despite minimal amino acid sequence identity, suggests divergence from a common, primordial ancestor in the evolution of terpene biosynthesis.

About this Structure

1DGP is a Single protein structure of sequence from Penicillium roqueforti with as ligand. Active as Aristolochene synthase, with EC number 4.2.3.9 Full crystallographic information is available from OCA.

Reference

Crystal structure determination of aristolochene synthase from the blue cheese mold, Penicillium roqueforti., Caruthers JM, Kang I, Rynkiewicz MJ, Cane DE, Christianson DW, J Biol Chem. 2000 Aug 18;275(33):25533-9. PMID:10825154

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