1w07
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The peroxisomal acyl-CoA oxidase family plays an essential role in lipid, metabolism by catalyzing the conversion of acyl-CoA into trans-2-enoyl-CoA, during fatty acid beta-oxidation. Here, we report the X-ray structure of, the FAD-containing Arabidopsis thaliana acyl-CoA oxidase 1 (ACX1), the, first three-dimensional structure of a plant acyl-CoA oxidase. Like other, acyl-CoA oxidases, the enzyme is a dimer and it has a fold resembling that, of mammalian acyl-CoA oxidase. A comparative analysis including mammalian, acyl-CoA oxidase and the related tetrameric mitochondrial acyl-CoA, dehydrogenases reveals a substrate-binding architecture that explains the, observed preference for long-chained, mono-unsaturated substrates in ACX1., Two anions are found at the ACX1 dimer interface and for .. | + | The peroxisomal acyl-CoA oxidase family plays an essential role in lipid, metabolism by catalyzing the conversion of acyl-CoA into trans-2-enoyl-CoA, during fatty acid beta-oxidation. Here, we report the X-ray structure of, the FAD-containing Arabidopsis thaliana acyl-CoA oxidase 1 (ACX1), the, first three-dimensional structure of a plant acyl-CoA oxidase. Like other, acyl-CoA oxidases, the enzyme is a dimer and it has a fold resembling that, of mammalian acyl-CoA oxidase. A comparative analysis including mammalian, acyl-CoA oxidase and the related tetrameric mitochondrial acyl-CoA, dehydrogenases reveals a substrate-binding architecture that explains the, observed preference for long-chained, mono-unsaturated substrates in ACX1., Two anions are found at the ACX1 dimer interface and for the first time, the presence of a disulfide bridge in a peroxisomal protein has been, observed. The functional differences between the peroxisomal acyl-CoA, oxidases and the mitochondrial acyl-CoA dehydrogenases are attributed to, structural differences in the FAD environments. |
==About this Structure== | ==About this Structure== | ||
| - | 1W07 is a | + | 1W07 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with CA, CL, PT and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Acyl-CoA_oxidase Acyl-CoA oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.3.6 1.3.3.6] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W07 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: peroxisomal beta-oxidation]] | [[Category: peroxisomal beta-oxidation]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:47:24 2007'' |
Revision as of 12:42, 5 November 2007
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ARABIDOPSIS THALIANA ACYL-COA OXIDASE 1
Overview
The peroxisomal acyl-CoA oxidase family plays an essential role in lipid, metabolism by catalyzing the conversion of acyl-CoA into trans-2-enoyl-CoA, during fatty acid beta-oxidation. Here, we report the X-ray structure of, the FAD-containing Arabidopsis thaliana acyl-CoA oxidase 1 (ACX1), the, first three-dimensional structure of a plant acyl-CoA oxidase. Like other, acyl-CoA oxidases, the enzyme is a dimer and it has a fold resembling that, of mammalian acyl-CoA oxidase. A comparative analysis including mammalian, acyl-CoA oxidase and the related tetrameric mitochondrial acyl-CoA, dehydrogenases reveals a substrate-binding architecture that explains the, observed preference for long-chained, mono-unsaturated substrates in ACX1., Two anions are found at the ACX1 dimer interface and for the first time, the presence of a disulfide bridge in a peroxisomal protein has been, observed. The functional differences between the peroxisomal acyl-CoA, oxidases and the mitochondrial acyl-CoA dehydrogenases are attributed to, structural differences in the FAD environments.
About this Structure
1W07 is a Single protein structure of sequence from Arabidopsis thaliana with CA, CL, PT and FAD as ligands. Active as Acyl-CoA oxidase, with EC number 1.3.3.6 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
Acyl-CoA oxidase 1 from Arabidopsis thaliana. Structure of a key enzyme in plant lipid metabolism., Pedersen L, Henriksen A, J Mol Biol. 2005 Jan 21;345(3):487-500. PMID:15581893
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