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

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 cofact...

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Autores principales: Azim, N., Deery, E., Warren, M. J., Erskine, P., Cooper, J. B., Wood, S. P., Akhtar, M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2013
Materias:
Crystallization Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3729171/
https://www.ncbi.nlm.nih.gov/pubmed/23908040
http://dx.doi.org/10.1107/S1744309113018526
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author Azim, N.
Deery, E.
Warren, M. J.
Erskine, P.
Cooper, J. B.
Wood, S. P.
Akhtar, M.
author_facet Azim, N.
Deery, E.
Warren, M. J.
Erskine, P.
Cooper, J. B.
Wood, S. P.
Akhtar, M.
author_sort Azim, N.
collection PubMed
description 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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spelling pubmed-37291712014-03-12 Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Bacillus megaterium Azim, N. Deery, E. Warren, M. J. Erskine, P. Cooper, J. B. Wood, S. P. Akhtar, M. Acta Crystallogr Sect F Struct Biol Cryst Commun Crystallization Communications 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. International Union of Crystallography 2013-07-27 /pmc/articles/PMC3729171/ /pubmed/23908040 http://dx.doi.org/10.1107/S1744309113018526 Text en © Azim et al. 2013 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
spellingShingle Crystallization Communications
Azim, N.
Deery, E.
Warren, M. J.
Erskine, P.
Cooper, J. B.
Wood, S. P.
Akhtar, M.
Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Bacillus megaterium
title Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Bacillus megaterium
title_full Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Bacillus megaterium
title_fullStr Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Bacillus megaterium
title_full_unstemmed Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Bacillus megaterium
title_short Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Bacillus megaterium
title_sort crystallization and preliminary x-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from bacillus megaterium
topic Crystallization Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3729171/
https://www.ncbi.nlm.nih.gov/pubmed/23908040
http://dx.doi.org/10.1107/S1744309113018526
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