1w07

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[[Image:1w07.gif|left|200px]]
[[Image:1w07.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1w07 |SIZE=350|CAPTION= <scene name='initialview01'>1w07</scene>, resolution 2.00&Aring;
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The line below this paragraph, containing "STRUCTURE_1w07", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Pt+Binding+Site+For+Chain+B'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1w07| PDB=1w07 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w07 OCA], [http://www.ebi.ac.uk/pdbsum/1w07 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w07 RCSB]</span>
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}}
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'''ARABIDOPSIS THALIANA ACYL-COA OXIDASE 1'''
'''ARABIDOPSIS THALIANA ACYL-COA OXIDASE 1'''
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[[Category: Henriksen, A.]]
[[Category: Henriksen, A.]]
[[Category: Pedersen, L.]]
[[Category: Pedersen, L.]]
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[[Category: fad cofactor]]
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[[Category: Fad cofactor]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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[[Category: peroxisomal beta-oxidation]]
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[[Category: Peroxisomal beta-oxidation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:58:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:29:22 2008''
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Revision as of 09:58, 3 May 2008

Template:STRUCTURE 1w07

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. 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 Sat May 3 12:58:51 2008

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