5eas

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==Overview==
==Overview==
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Terpene cyclases catalyze the synthesis of cyclic terpenes with 10-, 15-, and 20-carbon acyclic isoprenoid diphosphates as substrates. Plants have, been a source of these natural products by providing a homologous set of, terpene synthases. The crystal structures of 5-epi-aristolochene synthase, a sesquiterpene cyclase from tobacco, alone and complexed separately with, two farnesyl diphosphate analogs were analyzed. These structures reveal an, unexpected enzymatic mechanism for the synthesis of the bicyclic product, 5-epi-aristolochene, and provide a basis for understanding the, stereochemical selectivity displayed by other cyclases in the biosynthesis, of pharmacologically important cyclic terpenes. As such, these structures, provide templates for the engineering of novel terpene ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9295271 (full description)]]
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Terpene cyclases catalyze the synthesis of cyclic terpenes with 10-, 15-, and 20-carbon acyclic isoprenoid diphosphates as substrates. Plants have, been a source of these natural products by providing a homologous set of, terpene synthases. The crystal structures of 5-epi-aristolochene synthase, a sesquiterpene cyclase from tobacco, alone and complexed separately with, two farnesyl diphosphate analogs were analyzed. These structures reveal an, unexpected enzymatic mechanism for the synthesis of the bicyclic product, 5-epi-aristolochene, and provide a basis for understanding the, stereochemical selectivity displayed by other cyclases in the biosynthesis, of pharmacologically important cyclic terpenes. As such, these structures, provide templates for the engineering of novel terpene cyclases.
==About this Structure==
==About this Structure==
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5EAS is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Nicotiana_tabacum Nicotiana tabacum]] with MG as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Sites: MGA and MGB. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=5EAS OCA]].
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5EAS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Nicotiana_tabacum Nicotiana tabacum] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Sites: MGA and MGB. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=5EAS OCA].
==Reference==
==Reference==
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[[Category: natural products biosynthesis]]
[[Category: natural products biosynthesis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 17:48:53 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:05:14 2007''

Revision as of 10:59, 5 November 2007


5eas, resolution 2.25Å

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5-EPI-ARISTOLOCHENE SYNTHASE FROM NICOTIANA TABACUM

Overview

Terpene cyclases catalyze the synthesis of cyclic terpenes with 10-, 15-, and 20-carbon acyclic isoprenoid diphosphates as substrates. Plants have, been a source of these natural products by providing a homologous set of, terpene synthases. The crystal structures of 5-epi-aristolochene synthase, a sesquiterpene cyclase from tobacco, alone and complexed separately with, two farnesyl diphosphate analogs were analyzed. These structures reveal an, unexpected enzymatic mechanism for the synthesis of the bicyclic product, 5-epi-aristolochene, and provide a basis for understanding the, stereochemical selectivity displayed by other cyclases in the biosynthesis, of pharmacologically important cyclic terpenes. As such, these structures, provide templates for the engineering of novel terpene cyclases.

About this Structure

5EAS is a Single protein structure of sequence from Nicotiana tabacum with MG as ligand. Structure known Active Sites: MGA and MGB. Full crystallographic information is available from OCA.

Reference

Structural basis for cyclic terpene biosynthesis by tobacco 5-epi-aristolochene synthase., Starks CM, Back K, Chappell J, Noel JP, Science. 1997 Sep 19;277(5333):1815-20. PMID:9295271

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