2fon

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(New page: 200px<br /><applet load="2fon" size="350" color="white" frame="true" align="right" spinBox="true" caption="2fon, resolution 2.740&Aring;" /> '''X-ray crystal struc...)
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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Solanum lycopersicum]]
[[Category: Solanum lycopersicum]]
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[[Category: Garavito, R.M.]]
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[[Category: Garavito, R M.]]
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[[Category: Powers, R.A.]]
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[[Category: Powers, R A.]]
[[Category: FAD]]
[[Category: FAD]]
[[Category: fad cofactor]]
[[Category: fad cofactor]]
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[[Category: peroxisomal beta-oxidation]]
[[Category: peroxisomal beta-oxidation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 19:41:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:23:32 2008''

Revision as of 15:23, 21 February 2008


2fon, resolution 2.740Å

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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 with as ligand. Active as Acyl-CoA oxidase, with EC number 1.3.3.6 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

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