title: Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Arabidopsis thaliana.
abstract: The enzyme porphobilinogen deaminase (PBGD; hydroxymethylbilane synthase; EC 2.5.1.61) catalyses a key early step of the haem-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. Since PBGD catalyses a reaction which is common to the biosynthesis of both haem and chlorophyll, structural studies of a plant PBGD enzyme offer great potential for the discovery of novel herbicides. Until recently, structural data have only been available for the Escherichia coli and human forms of the enzyme. Expression in E. coli of a codon-optimized gene for Arabidopsis thaliana PBGD has permitted for the first time the crystallization and preliminary X-ray analysis of the enzyme from a plant species at high resolution.
authors.affiliation: School of Biological Sciences, University of Southampton, Southampton SO16 7PX, England.
authors.forename: A
authors.initials: A
authors.lastname: Roberts
authors.forename: R
authors.initials: R
authors.lastname: Gill
authors.forename: R J
authors.initials: RJ
authors.lastname: Hussey
authors.forename: H
authors.initials: H
authors.lastname: Mikolajek
authors.forename: P T
authors.initials: PT
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: E J T
authors.initials: EJ
authors.lastname: Chrystal
authors.forename: P M
authors.initials: PM
authors.lastname: Shoolingin-Jordan
mesh_terms: D017360:Arabidopsis / Q000201:enzymology* / Q000378:metabolism; D029681:Arabidopsis Proteins / Q000737:chemistry* / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D011163:Hydroxymethylbilane Synthase / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D011162:Porphobilinogen / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D045725:Tetrapyrroles / Q000096:biosynthesis* / Q000737:chemistry
chemical_list: D029681:Arabidopsis Proteins; D045725:Tetrapyrroles; C056776:dipyrromethane cofactor; D011162:Porphobilinogen; D011163:Hydroxymethylbilane Synthase