PMID:1522882

Citation	Louie, GV, Brownlie, PD, Lambert, R, Cooper, JB, Blundell, TL, Wood, SP, Warren, MJ, Woodcock, SC and Jordan, PM (1992) Structure of porphobilinogen deaminase reveals a flexible multidomain polymerase with a single catalytic site. Nature 359:33-9
Abstract	The three-domain structure of porphobilinogen deaminase, a key enzyme in the biosynthetic pathway of tetrapyrroles, has been defined by X-ray analysis at 1.9 A resolution. Two of the domains structurally resemble the transferrins and periplasmic binding proteins. The dipyrromethane cofactor is covalently linked to domain 3 but is bound by extensive salt-bridges and hydrogen-bonds within the cleft between domains 1 and 2, at a position corresponding to the binding sites for small-molecule ligands in the analogous proteins. The X-ray structure and results from site-directed mutagenesis provide evidence for a single catalytic site. Interdomain flexibility may aid elongation of the polypyrrole product in the active-site cleft of the enzyme.
Links	PubMed Online version:10.1038/359033a0
Keywords	Binding Sites; Coenzymes/chemistry; Hydroxymethylbilane Synthase/chemistry; Models, Molecular; Molecular Structure; Porphobilinogen/chemistry; Protein Conformation
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