1zdy

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(New page: 200px<br /><applet load="1zdy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zdy, resolution 1.44&Aring;" /> '''Co-crystal structure...)
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[[Image:1zdy.gif|left|200px]]<br /><applet load="1zdy" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="1zdy, resolution 1.44&Aring;" />
'''Co-crystal structure of Orf2 an aromatic prenyl transferase from Streptomyces sp. strain CL190 complexed with TAPS'''<br />
'''Co-crystal structure of Orf2 an aromatic prenyl transferase from Streptomyces sp. strain CL190 complexed with TAPS'''<br />
==Overview==
==Overview==
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The anti-oxidant naphterpin is a natural product containing a, polyketide-based aromatic core with an attached 10-carbon geranyl group, derived from isoprenoid (terpene) metabolism. Hybrid natural products such, as naphterpin that contain 5-carbon (dimethylallyl), 10-carbon (geranyl), or 15-carbon (farnesyl) isoprenoid chains possess biological activities, distinct from their non-prenylated aromatic precursors. These hybrid, natural products represent new anti-microbial, anti-oxidant, anti-inflammatory, anti-viral and anti-cancer compounds. A small number of, aromatic prenyltransferases (PTases) responsible for prenyl group, attachment have only recently been isolated and characterized. Here we, report the gene identification, biochemical characterization and, high-resolution X-ray crystal structures of an architecturally novel, aromatic PTase, Orf2 from Streptomyces sp. strain CL190, with substrates, and substrate analogues bound. In vivo, Orf2 attaches a geranyl group to a, 1,3,6,8-tetrahydroxynaphthalene-derived polyketide during naphterpin, biosynthesis. In vitro, Orf2 catalyses carbon-carbon-based and, carbon-oxygen-based prenylation of a diverse collection of, hydroxyl-containing aromatic acceptors of synthetic, microbial and plant, origin. These crystal structures, coupled with in vitro assays, provide a, basis for understanding and potentially manipulating the regio-specific, prenylation of aromatic small molecules using this structurally unique, family of aromatic PTases.
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The anti-oxidant naphterpin is a natural product containing a polyketide-based aromatic core with an attached 10-carbon geranyl group derived from isoprenoid (terpene) metabolism. Hybrid natural products such as naphterpin that contain 5-carbon (dimethylallyl), 10-carbon (geranyl) or 15-carbon (farnesyl) isoprenoid chains possess biological activities distinct from their non-prenylated aromatic precursors. These hybrid natural products represent new anti-microbial, anti-oxidant, anti-inflammatory, anti-viral and anti-cancer compounds. A small number of aromatic prenyltransferases (PTases) responsible for prenyl group attachment have only recently been isolated and characterized. Here we report the gene identification, biochemical characterization and high-resolution X-ray crystal structures of an architecturally novel aromatic PTase, Orf2 from Streptomyces sp. strain CL190, with substrates and substrate analogues bound. In vivo, Orf2 attaches a geranyl group to a 1,3,6,8-tetrahydroxynaphthalene-derived polyketide during naphterpin biosynthesis. In vitro, Orf2 catalyses carbon-carbon-based and carbon-oxygen-based prenylation of a diverse collection of hydroxyl-containing aromatic acceptors of synthetic, microbial and plant origin. These crystal structures, coupled with in vitro assays, provide a basis for understanding and potentially manipulating the regio-specific prenylation of aromatic small molecules using this structurally unique family of aromatic PTases.
==About this Structure==
==About this Structure==
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1ZDY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Streptomyces_sp._cl190 Streptomyces sp. cl190] with T3A as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZDY OCA].
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1ZDY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Streptomyces_sp._cl190 Streptomyces sp. cl190] with <scene name='pdbligand=T3A:'>T3A</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZDY OCA].
==Reference==
==Reference==
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[[Category: Streptomyces sp. cl190]]
[[Category: Streptomyces sp. cl190]]
[[Category: Kuzuyama, T.]]
[[Category: Kuzuyama, T.]]
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[[Category: Noel, J.P.]]
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[[Category: Noel, J P.]]
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[[Category: Richard, S.B.]]
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[[Category: Richard, S B.]]
[[Category: T3A]]
[[Category: T3A]]
[[Category: novel aromatic prenyltransferase barrel fold]]
[[Category: novel aromatic prenyltransferase barrel fold]]
[[Category: pt-barrel]]
[[Category: pt-barrel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 04:50:20 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:14:37 2008''

Revision as of 14:14, 21 February 2008


1zdy, resolution 1.44Å

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Co-crystal structure of Orf2 an aromatic prenyl transferase from Streptomyces sp. strain CL190 complexed with TAPS

Overview

The anti-oxidant naphterpin is a natural product containing a polyketide-based aromatic core with an attached 10-carbon geranyl group derived from isoprenoid (terpene) metabolism. Hybrid natural products such as naphterpin that contain 5-carbon (dimethylallyl), 10-carbon (geranyl) or 15-carbon (farnesyl) isoprenoid chains possess biological activities distinct from their non-prenylated aromatic precursors. These hybrid natural products represent new anti-microbial, anti-oxidant, anti-inflammatory, anti-viral and anti-cancer compounds. A small number of aromatic prenyltransferases (PTases) responsible for prenyl group attachment have only recently been isolated and characterized. Here we report the gene identification, biochemical characterization and high-resolution X-ray crystal structures of an architecturally novel aromatic PTase, Orf2 from Streptomyces sp. strain CL190, with substrates and substrate analogues bound. In vivo, Orf2 attaches a geranyl group to a 1,3,6,8-tetrahydroxynaphthalene-derived polyketide during naphterpin biosynthesis. In vitro, Orf2 catalyses carbon-carbon-based and carbon-oxygen-based prenylation of a diverse collection of hydroxyl-containing aromatic acceptors of synthetic, microbial and plant origin. These crystal structures, coupled with in vitro assays, provide a basis for understanding and potentially manipulating the regio-specific prenylation of aromatic small molecules using this structurally unique family of aromatic PTases.

About this Structure

1ZDY is a Protein complex structure of sequences from Streptomyces sp. cl190 with as ligand. Full crystallographic information is available from OCA.

Reference

Structural basis for the promiscuous biosynthetic prenylation of aromatic natural products., Kuzuyama T, Noel JP, Richard SB, Nature. 2005 Jun 16;435(7044):983-7. PMID:15959519

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