Expression, crystallization and preliminary X-ray analysis of McbB, a multifunctional enzyme involved in β-carboline skeleton biosynthesis

Acta Crystallogr F Struct Biol Commun. 2014 Oct;70(Pt 10):1402-5. doi: 10.1107/S2053230X14018743. Epub 2014 Sep 25.

Abstract

β-Carboline alkaloids (βCs), with tricyclic pyrido[3,4-b]indole rings, have important pharmacological and therapeutic value. In the biosynthesis of βCs, 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 2.10 Å resolution and belonged to the monoclinic space group P21, with unit-cell parameters a = 66.06, b = 85.48, c = 106.19 Å, α = 90.00, β = 106.77, γ = 90.00°. These results provide a basis for solving the crystal structure and elucidating the catalytic mechanism for McbB.

Keywords: Marinactinospora thermotolerans; McbB; Pictet–Spengler cyclization; β-carboline alkaloids.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actinobacteria / enzymology*
  • Amino Acid Sequence
  • Bacterial Proteins / biosynthesis
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / isolation & purification
  • Carbolines / metabolism
  • Chromatography, Affinity
  • Crystallization
  • Crystallography, X-Ray
  • Gene Expression
  • Molecular Sequence Data
  • Multifunctional Enzymes / biosynthesis
  • Multifunctional Enzymes / chemistry*
  • Multifunctional Enzymes / isolation & purification

Substances

  • Bacterial Proteins
  • Carbolines
  • Multifunctional Enzymes