Structure of porphobilinogen deaminase reveals a flexible multidomain polymerase with a single catalytic site

Gordon V. Louie, Paul D. Brownlie, Richard Lambert, Jonathan B. Cooper, Tom L. Blundell, Steve P. Wood, Martin J. Warren, Sarah C. Woodcock, Peter M. Jordan

Research output: Contribution to journalArticlepeer-review

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 Å 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.
Original languageEnglish
Pages (from-to)33-39
JournalNature
Volume359
Issue number6390
DOIs
Publication statusPublished - 3 Sep 1992

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