1wx2
From Proteopedia
(New page: 200px<br /><applet load="1wx2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wx2, resolution 1.80Å" /> '''Crystal Structure of...) |
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| - | [[Image:1wx2.gif|left|200px]]<br /><applet load="1wx2" size=" | + | [[Image:1wx2.gif|left|200px]]<br /><applet load="1wx2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wx2, resolution 1.80Å" /> | caption="1wx2, resolution 1.80Å" /> | ||
'''Crystal Structure of the oxy-form of the copper-bound Streptomyces castaneoglobisporus tyrosinase complexed with a caddie protein prepared by the addition of hydrogenperoxide'''<br /> | '''Crystal Structure of the oxy-form of the copper-bound Streptomyces castaneoglobisporus tyrosinase complexed with a caddie protein prepared by the addition of hydrogenperoxide'''<br /> | ||
==Overview== | ==Overview== | ||
| - | At high resolution, we determined the crystal structures of copper-bound | + | At high resolution, we determined the crystal structures of copper-bound and metal-free tyrosinase in a complex with ORF378 designated as a "caddie" protein because it assists with transportation of two CuII ions into the tyrosinase catalytic center. These structures suggest that the caddie protein covers the hydrophobic molecular surface of tyrosinase and interferes with the binding of a substrate tyrosine to the catalytic site of tyrosinase. The caddie protein, which consists of one six-strandedbeta-sheet and one alpha-helix, has no similarity with all proteins deposited into the Protein Data Bank. Although tyrosinase and catechol oxidase are classified into the type 3 copper protein family, the latter enzyme lacks monooxygenase activity. The difference in catalytic activity is based on the structural observations that a large vacant space is present just above the active center of tyrosinase and that one of the six His ligands for the two copper ions is highly flexible. These structural characteristics of tyrosinase suggest that, in the reaction that catalyzes the ortho-hydroxylation of monophenol, one of the two Cu(II) ions is coordinated by the peroxide-originated oxygen bound to the substrate. Our crystallographic study shows evidence that the tyrosinase active center formed by dinuclear coppers is flexible during catalysis. |
==About this Structure== | ==About this Structure== | ||
| - | 1WX2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Streptomyces_castaneoglobisporus Streptomyces castaneoglobisporus] with CU, NO3 and PER as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Monophenol_monooxygenase Monophenol monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.18.1 1.14.18.1] Full crystallographic information is available from [http:// | + | 1WX2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Streptomyces_castaneoglobisporus Streptomyces castaneoglobisporus] with <scene name='pdbligand=CU:'>CU</scene>, <scene name='pdbligand=NO3:'>NO3</scene> and <scene name='pdbligand=PER:'>PER</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Monophenol_monooxygenase Monophenol monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.18.1 1.14.18.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WX2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: tyrosinase]] | [[Category: tyrosinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:48:57 2008'' |
Revision as of 13:48, 21 February 2008
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Crystal Structure of the oxy-form of the copper-bound Streptomyces castaneoglobisporus tyrosinase complexed with a caddie protein prepared by the addition of hydrogenperoxide
Overview
At high resolution, we determined the crystal structures of copper-bound and metal-free tyrosinase in a complex with ORF378 designated as a "caddie" protein because it assists with transportation of two CuII ions into the tyrosinase catalytic center. These structures suggest that the caddie protein covers the hydrophobic molecular surface of tyrosinase and interferes with the binding of a substrate tyrosine to the catalytic site of tyrosinase. The caddie protein, which consists of one six-strandedbeta-sheet and one alpha-helix, has no similarity with all proteins deposited into the Protein Data Bank. Although tyrosinase and catechol oxidase are classified into the type 3 copper protein family, the latter enzyme lacks monooxygenase activity. The difference in catalytic activity is based on the structural observations that a large vacant space is present just above the active center of tyrosinase and that one of the six His ligands for the two copper ions is highly flexible. These structural characteristics of tyrosinase suggest that, in the reaction that catalyzes the ortho-hydroxylation of monophenol, one of the two Cu(II) ions is coordinated by the peroxide-originated oxygen bound to the substrate. Our crystallographic study shows evidence that the tyrosinase active center formed by dinuclear coppers is flexible during catalysis.
About this Structure
1WX2 is a Protein complex structure of sequences from Streptomyces castaneoglobisporus with , and as ligands. Active as Monophenol monooxygenase, with EC number 1.14.18.1 Full crystallographic information is available from OCA.
Reference
Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis., Matoba Y, Kumagai T, Yamamoto A, Yoshitsu H, Sugiyama M, J Biol Chem. 2006 Mar 31;281(13):8981-90. Epub 2006 Jan 25. PMID:16436386
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