Expression, crystallization and preliminary X-ray analysis of McbB, a multifunctional enzyme involved in [beta]-carboline skeleton biosynthesis
[beta]-Carboline alkaloids ([beta]Cs), with tricyclic pyrido[3,4-b]indole rings, have important pharmacological and therapeutic value. In the biosynthesis of [beta]Cs, the Pictet-Spengler (PS) cyclization reaction is responsible for the formation of ring structures. McbB is one of a few enzymes that...
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| Veröffentlicht in: | Acta crystallographica. Section F, Structural biology communications Structural biology communications, 2014-10, Vol.70 (10), p.1402 |
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| container_title | Acta crystallographica. Section F, Structural biology communications |
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| creator | Wang, Hua Zhang, Huaidong Mi, Yanling Ju, Jianhua Chen, Qi Zhang, Houjin |
| description | [beta]-Carboline alkaloids ([beta]Cs), with tricyclic pyrido[3,4-b]indole rings, have important pharmacological and therapeutic value. In the biosynthesis of [beta]Cs, the Pictet-Spengler (PS) cyclization reaction is responsible for the formation of ring structures. McbB is one of a few enzymes that are known to catalyse PS cyclization. It can also catalyse decarboxylation and oxidation. Here, the expression, crystallization and preliminary data analysis of McbB are reported. The crystals diffracted to 2.10Å resolution and belonged to the monoclinic space group P21, with unit-cell parameters a = 66.06, b = 85.48, c = 106.19Å, [alpha] = 90.00, [beta] = 106.77, [gamma] = 90.00°. These results provide a basis for solving the crystal structure and elucidating the catalytic mechanism for McbB. [PUBLICATION ABSTRACT] |
| doi_str_mv | 10.1107/S2053230X14018743 |
| format | Article |
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In the biosynthesis of [beta]Cs, the Pictet-Spengler (PS) cyclization reaction is responsible for the formation of ring structures. McbB is one of a few enzymes that are known to catalyse PS cyclization. It can also catalyse decarboxylation and oxidation. Here, the expression, crystallization and preliminary data analysis of McbB are reported. The crystals diffracted to 2.10Å resolution and belonged to the monoclinic space group P21, with unit-cell parameters a = 66.06, b = 85.48, c = 106.19Å, [alpha] = 90.00, [beta] = 106.77, [gamma] = 90.00°. These results provide a basis for solving the crystal structure and elucidating the catalytic mechanism for McbB. [PUBLICATION ABSTRACT]</description><identifier>EISSN: 2053-230X</identifier><identifier>DOI: 10.1107/S2053230X14018743</identifier><language>eng</language><publisher>Chester: Wiley Subscription Services, Inc</publisher><ispartof>Acta crystallographica. 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Section F, Structural biology communications</title><description>[beta]-Carboline alkaloids ([beta]Cs), with tricyclic pyrido[3,4-b]indole rings, have important pharmacological and therapeutic value. In the biosynthesis of [beta]Cs, the Pictet-Spengler (PS) cyclization reaction is responsible for the formation of ring structures. McbB is one of a few enzymes that are known to catalyse PS cyclization. It can also catalyse decarboxylation and oxidation. Here, the expression, crystallization and preliminary data analysis of McbB are reported. The crystals diffracted to 2.10Å resolution and belonged to the monoclinic space group P21, with unit-cell parameters a = 66.06, b = 85.48, c = 106.19Å, [alpha] = 90.00, [beta] = 106.77, [gamma] = 90.00°. These results provide a basis for solving the crystal structure and elucidating the catalytic mechanism for McbB. 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| title | Expression, crystallization and preliminary X-ray analysis of McbB, a multifunctional enzyme involved in [beta]-carboline skeleton biosynthesis |
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