1bt2: Difference between revisions

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==Overview==
==Overview==
Catechol oxidases are ubiquitous plant enzymes containing a dinuclear, copper center. In the wound-response mechanism of the plant they catalyze, the oxidation of a broad range of ortho-diphenols to the corresponding, o-quinones coupled with the reduction of oxygen to water. The crystal, structures of the enzyme from sweet potato in the resting dicupric, Cu(II)-Cu(II) state, the reduced dicuprous Cu(I)-Cu(I) form, and in, complex with the inhibitor phenylthiourea were analyzed. The catalytic, copper center is accommodated in a central four-helix-bundle located in a, hydrophobic pocket close to the surface. Both metal binding sites are, composed of three histidine ligands. His 109, ligated to the CuA site, is, covalently linked to Cys 92 by an unusual thioether bond. Based on, biochemical, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9846879 (full description)]]
Catechol oxidases are ubiquitous plant enzymes containing a dinuclear, copper center. In the wound-response mechanism of the plant they catalyze, the oxidation of a broad range of ortho-diphenols to the corresponding, o-quinones coupled with the reduction of oxygen to water. The crystal, structures of the enzyme from sweet potato in the resting dicupric, Cu(II)-Cu(II) state, the reduced dicuprous Cu(I)-Cu(I) form, and in, complex with the inhibitor phenylthiourea were analyzed. The catalytic, copper center is accommodated in a central four-helix-bundle located in a, hydrophobic pocket close to the surface. Both metal binding sites are, composed of three histidine ligands. His 109, ligated to the CuA site, is, covalently linked to Cys 92 by an unusual thioether bond. Based on, biochemical, spectroscopic and the presented structural data, a, catalytical mechanism is proposed in which one of the oxygen atoms of the, diphenolic substrate binds to CuB of the oxygenated enzyme.


==About this Structure==
==About this Structure==
1BT2 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Ipomoea_batatas Ipomoea batatas]] with C2O as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Catechol_oxidase Catechol oxidase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.3.1 1.10.3.1]]. Structure known Active Sites: CU1, CU2, CU3 and CU4. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BT2 OCA]].  
1BT2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ipomoea_batatas Ipomoea batatas] with C2O as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Catechol_oxidase Catechol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.3.1 1.10.3.1] Structure known Active Sites: CU1, CU2, CU3 and CU4. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BT2 OCA].  


==Reference==
==Reference==
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[[Category: ipomoea batatas]]
[[Category: ipomoea batatas]]


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