1di1

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(New page: 200px<br /><applet load="1di1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1di1, resolution 2.5&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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caption="1di1, resolution 2.5&Aring;" />
'''CRYSTAL STRUCTURE OF ARISTOLOCHENE SYNTHASE FROM PENICILLIUM ROQUEFORTI'''<br />
'''CRYSTAL STRUCTURE OF ARISTOLOCHENE SYNTHASE FROM PENICILLIUM ROQUEFORTI'''<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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1DI1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Penicillium_roqueforti Penicillium roqueforti]. 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=1DI1 OCA].
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1DI1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Penicillium_roqueforti Penicillium roqueforti]. 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=1DI1 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.]]
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[[Category: Rynkiewicz, M.J.]]
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[[Category: Rynkiewicz, M J.]]
[[Category: isoprenoid biosynthesis]]
[[Category: isoprenoid biosynthesis]]
[[Category: sesquiterpene cyclase]]
[[Category: sesquiterpene cyclase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:16:43 2008''

Revision as of 10:16, 21 February 2008


1di1, resolution 2.5Å

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CRYSTAL STRUCTURE OF ARISTOLOCHENE SYNTHASE FROM PENICILLIUM ROQUEFORTI

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

1DI1 is a Single protein structure of sequence from Penicillium roqueforti. 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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