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

@article{Schubert2008StructureAM,
  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},
  journal={Biochemistry},
  year={2008},
  volume={47 33},
  pages={8648-55}
}
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

From This Paper

Topics from this paper.

Citations

Publications citing this paper.
Showing 1-9 of 9 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 35 references

A solution for the best rotation to relate two sets of vectors

  • W. Kabsch
  • Acta Crystallogr., A
  • 1976
Highly Influential
2 Excerpts

Identification and characterization of the Arabidopsis gene encoding the tetrapyrrole biosynthesis enzyme uroporphyrinogen III synthase

  • Tan, F.-C, +5 authors A. G. Smith
  • Biochem . J .
  • 2007
1 Excerpt

Crystal structure of uroporphyrinogen III synthase from an extremely thermophilic bacterium Thermus thermophilus HB 8 . Unpublished

  • F. Studier
  • 2005

Similar Papers

Loading similar papers…