This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1w07
From Proteopedia
| Line 5: | Line 5: | ||
==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== | ||
| Line 25: | Line 25: | ||
[[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
|
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
Page seeded by OCA on Mon Nov 5 14:47:24 2007
