1zdy
From Proteopedia
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| - | [[Image:1zdy.gif|left|200px]] | + | [[Image:1zdy.gif|left|200px]] |
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| - | '''Co-crystal structure of Orf2 an aromatic prenyl transferase from Streptomyces sp. strain CL190 complexed with TAPS''' | + | {{Structure |
| + | |PDB= 1zdy |SIZE=350|CAPTION= <scene name='initialview01'>1zdy</scene>, resolution 1.44Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=T3A:N-(TRIS(HYDROXYMETHYL)METHYL)-3-AMINOPROPANESULFONIC ACID'>T3A</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Co-crystal structure of Orf2 an aromatic prenyl transferase from Streptomyces sp. strain CL190 complexed with TAPS''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ZDY is a [ | + | 1ZDY is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Streptomyces_sp._cl190 Streptomyces sp. cl190]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZDY OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15959519 15959519] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Streptomyces sp. cl190]] | [[Category: Streptomyces sp. cl190]] | ||
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[[Category: pt-barrel]] | [[Category: pt-barrel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:34:18 2008'' |
Revision as of 13:34, 20 March 2008
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| , resolution 1.44Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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