2fon: Difference between revisions

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New page: left|200px<br /><applet load="2fon" size="350" color="white" frame="true" align="right" spinBox="true" caption="2fon, resolution 2.740Å" /> '''X-ray crystal struc...
 
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==Overview==
==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.
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]]
[[Category: Garavito, R.M.]]
[[Category: Garavito, R M.]]
[[Category: Powers, R.A.]]
[[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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