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

Research output: Contribution to journalArticle

  • Gordon V. Louie
  • Paul D. Brownlie
  • Richard Lambert
  • Jonathan B. Cooper
  • Tom L. Blundell
  • Professor Steve Wood
  • Martin J. Warren
  • Sarah C. Woodcock
  • Peter M. Jordan
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
Issue number6390
Publication statusPublished - 3 Sep 1992

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