title: Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Bacillus megaterium.
abstract: The enzyme porphobilinogen deaminase (PBGD; hydroxymethylbilane synthase; EC 2.5.1.61) catalyses an early step of the tetrapyrrole-biosynthesis pathway in which four molecules of the monopyrrole porphobilinogen are condensed to form a linear tetrapyrrole. The enzyme possesses a dipyrromethane cofactor which is covalently linked by a thioether bridge to an invariant cysteine residue. Expression in Escherichia coli of a His-tagged form of Bacillus megaterium PBGD permitted the crystallization and preliminary X-ray analysis of the enzyme from this species at high resolution.
authors.affiliation: School of Biological Sciences, University of Punjab, New Campus, Lahore 54590, Pakistan.
authors.forename: N
authors.initials: N
authors.lastname: Azim
authors.forename: E
authors.initials: E
authors.lastname: Deery
authors.forename: M J
authors.initials: MJ
authors.lastname: Warren
authors.forename: P
authors.initials: P
authors.lastname: Erskine
authors.forename: J B
authors.initials: JB
authors.lastname: Cooper
authors.forename: S P
authors.initials: SP
authors.lastname: Wood
authors.forename: M
authors.initials: M
authors.lastname: Akhtar
mesh_terms: D001410:Bacillus megaterium / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D011163:Hydroxymethylbilane Synthase / Q000737:chemistry*; D045725:Tetrapyrroles / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D045725:Tetrapyrroles; D011163:Hydroxymethylbilane Synthase
keywords: Bacillus megaterium; dipyrromethane cofactor; porphobilinogen deaminase; tetrapyrrole biosynthesis
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