Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Bacillus megaterium.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 69(Pt 8): 906-8, 2013 Aug.
Article
em En
| MEDLINE
| ID: mdl-23908040
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.
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Base de dados:
MEDLINE
Assunto principal:
Hidroximetilbilano Sintase
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Bacillus megaterium
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Proteínas de Bactérias
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Tetrapirróis
Idioma:
En
Ano de publicação:
2013
Tipo de documento:
Article