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

@article{Louie1992StructureOP,
  title={Structure of porphobilinogen deaminase reveals a flexible multidomain polymerase with a single catalytic site},
  author={Gordon V. Louie and Paul D. Brownlie and Richard H. Lambert and Jonathan B. Cooper and Tom L. Blundell and Steve P. Wood and Martin J. Warren and Sarah C. Woodcock and Peter M. Shoolingin Jordan},
  journal={Nature},
  year={1992},
  volume={359},
  pages={33-39}
}
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… CONTINUE READING

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