Crystal structure of Agaricus bisporus mushroom tyrosinase: identity of the tetramer subunits and interaction with tropolone
| العنوان: | Crystal structure of Agaricus bisporus mushroom tyrosinase: identity of the tetramer subunits and interaction with tropolone |
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| المؤلفون: | Harry J. Wichers, Jurriaan J. Mes, Henriëtte J. Rozeboom, Bauke W. Dijkstra, A. Weijn, Wangsa T. Ismaya, Fabrizia Fusetti |
| المساهمون: | X-ray Crystallography, Enzymology |
| المصدر: | Biochemistry 50 (2011) 24 Biochemistry, 50(24), 5477-5486. AMER CHEMICAL SOC Biochemistry, 50(24), 5477-5486 |
| سنة النشر: | 2011 |
| مصطلحات موضوعية: | MECHANISM, Models, Molecular, Protein Folding, POLYPHENOL OXIDASE, Tyrosinase, Agaricus, PROTEIN, plant, Crystallography, X-Ray, 01 natural sciences, Biochemistry, Substrate Specificity, ACTIVATION, chemistry.chemical_compound, Protein structure, Catalytic Domain, FBR Fresh Supply Chains, refinement, DNA, Fungal, 2. Zero hunger, 0303 health sciences, Food Chemistry, REFINEMENT, biology, Chemistry, Monophenol Monooxygenase, Fungal genetics, Tropolone, inhibition, Protein Binding, Stereochemistry, Protein subunit, Molecular Sequence Data, INHIBITION, mechanism, Celbiologie en Immunologie, SEQUENCE, 03 medical and health sciences, DIFFRACTION DATA, Tetramer, diffraction data, Levensmiddelenchemie, Amino Acid Sequence, PLANT, polyphenol oxidase, Protein Structure, Quaternary, Histidine, 030304 developmental biology, Binding Sites, Base Sequence, Sequence Homology, Amino Acid, 010405 organic chemistry, Active site, sequence, MULTIPLE FORMS, multiple forms, 0104 chemical sciences, Protein Subunits, Cell Biology and Immunology, biology.protein, activation, protein, Copper |
| الوصف: | Tyrosinase catalyzes the conversion of phenolic compounds into their quinone derivatives, which are precursors for the formation of melanin, a ubiquitous pigment in living organisms. Because of its importance for browning reactions in the food industry, the tyrosinase from the mushroom Agaricus bisporus has been investigated in depth. In previous studies the tyrosinase enzyme complex was shown to be a H(2)L(2) tetramer, but no clues were obtained of the identities of the subunits, their mode of association, and the 3D structure of he complex. Here we unravel this tetramer at the molecular level. Its 2.3 angstrom resolution crystal structure is the first structure of the full fungal tyrosinase complex. The complex comprises two H subunits of similar to 392 residues and two L subunits of similar to 150 residues. The H subunit originates from the ppo3 gene and has a fold similar to other tyrosinases, but it is similar to 100 residues larger. The L subunit appeared to be the product of orf239342 and has a lectin-like fold. The H subunit contains a binuclear copper-binding site in the deoxy-state, in which three histidine residues coordinate each copper ion. The side chains of these histidines have their orientation fixed by hydrogen bonds or, in the case of His85, by a thioether bridge with the side chain of Cys83. The specific tyrosinase inhibitor tropolone forms a pre-Michaelis complex with the enzyme. It binds near the binuclear copper site without directly coordinating the copper ions. The function of the ORF239342 subunits is not known. Carbohydrate binding sites identified in other lectins are not conserved in ORF239342, and the subunits are over 25 angstrom away from the active site, making a role in activity unlikely. The structures explain how calcium ions stabilize the tetrameric state of the enzyme. |
| وصف الملف: | application/pdf; application/octet-stream |
| تدمد: | 1520-4995 0006-2960 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::acb5079ecde258ef2a8fe6d85b85f2c9Test https://pubmed.ncbi.nlm.nih.gov/21598903Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....acb5079ecde258ef2a8fe6d85b85f2c9 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 15204995 00062960 |
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