2fon
From Proteopedia
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|PDB= 2fon |SIZE=350|CAPTION= <scene name='initialview01'>2fon</scene>, resolution 2.740Å | |PDB= 2fon |SIZE=350|CAPTION= <scene name='initialview01'>2fon</scene>, resolution 2.740Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene> | + | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> |
| - | |ACTIVITY= [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] | + | |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> |
|GENE= ACX1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4081 Solanum lycopersicum]) | |GENE= ACX1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4081 Solanum lycopersicum]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fon OCA], [http://www.ebi.ac.uk/pdbsum/2fon PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fon RCSB]</span> | ||
}} | }} | ||
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[[Category: Garavito, R M.]] | [[Category: Garavito, R M.]] | ||
[[Category: Powers, R A.]] | [[Category: Powers, R A.]] | ||
| - | [[Category: FAD]] | ||
[[Category: fad cofactor]] | [[Category: fad cofactor]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
[[Category: peroxisomal beta-oxidation]] | [[Category: peroxisomal beta-oxidation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:05:38 2008'' |
Revision as of 00:05, 31 March 2008
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| , resolution 2.740Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | ACX1A (Solanum lycopersicum) | ||||||
| Activity: | Acyl-CoA oxidase, with EC number 1.3.3.6 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-ray crystal structure of LeACX1, an acyl-CoA oxidase from Lycopersicon esculentum (tomato)
Overview
The flavoenzyme acyl-CoA oxidase (ACX) catalyzes the first committed step in beta-oxidation and is required for the biosynthesis of jasmonic acid, a signaling molecule involved in plant defense. Recently, a mutant in tomato was identified that is deficient in jasmonic acid production and compromised in its wound response. This results from a single point mutation in acx1, which causes the conserved residue Thr138 to be substituted by isoleucine. To understand the structural basis for this mutation, the crystal structure of LeACX1 was determined to 2.74 Angstrom resolution by molecular replacement. Unexpectedly, an unusual packing arrangement was observed in which three monomers of LeACX1 are present in the asymmetric unit. Although the tertiary structure of LeACX1 is essentially similar to the previously determined structures of ACX enzymes, the packing within the unit cells is distinctly different.
About this Structure
2FON is a Single protein structure of sequence from Solanum lycopersicum. Full crystallographic information is available from OCA.
Reference
Structure determination and analysis of acyl-CoA oxidase (ACX1) from tomato., Powers RA, Rife CL, Schilmiller AL, Howe GA, Garavito RM, Acta Crystallogr D Biol Crystallogr. 2006 Jun;62(Pt 6):683-6. Epub 2006, May 12. PMID:16699197
Page seeded by OCA on Mon Mar 31 03:05:38 2008
