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Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Bacillus megaterium

DOI: 10.1107/S1744309113018526 DOI Help
PMID: 23908040 PMID Help

Authors: N. Azim (University of Punjab) , E. Deery (University of Kent) , M J. Warren (University of Kent) , P. Erskine (UCL Division of Medicine (Royal Free Campus)) , J. B. Cooper (UCL Division of Medicine (Royal Free Campus)) , S. P. Wood (UCL Division of Medicine (Royal Free Campus)) , M. Akhtar (University of Punjab)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology And Crystallization Communications , VOL 69 , PAGES 906 - 908

State: Published (Approved)
Published: August 2013
Diamond Proposal Number(s): 7131

Open Access Open Access

Abstract: The enzyme porphobilinogen deaminase (PBGD; hydroxymethylbilane synthase; EC 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.

Journal Keywords: The Enzyme Porphobilinogen Deaminase (Pbgd; Hydroxymethylbilane

Subject Areas: Biology and Bio-materials

Instruments: I03-Macromolecular Crystallography

Added On: 06/08/2013 15:32

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