Structure and mechanistic implications of a uroporphyrinogen III synthase-product complex.

  title={Structure and mechanistic implications of a uroporphyrinogen III synthase-product complex.},
  author={Heidi L. Schubert and John D. Phillips and Annie H{\'e}roux and Christopher P Hill},
  volume={47 33},
Uroporphyrinogen III synthase (U3S) catalyzes the asymmetrical cyclization of a linear tetrapyrrole to form the physiologically relevant uroporphyrinogen III (uro'gen III) isomer during heme biosynthesis. Here, we report four apoenzyme and one product complex crystal structures of the Thermus thermophilus (HB27) U3S protein. The overlay of eight crystallographically unique U3S molecules reveals a huge range of conformational flexibility, including a "closed" product complex. The product, uro… CONTINUE READING

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