Nature Communications (Apr 2020)

Allosteric regulation accompanied by oligomeric state changes of Trypanosoma brucei GMP reductase through cystathionine-β-synthase domain

  • Akira Imamura,
  • Tetsuya Okada,
  • Hikaru Mase,
  • Takuya Otani,
  • Tomoka Kobayashi,
  • Manatsu Tamura,
  • Bruno Kilunga Kubata,
  • Katsuaki Inoue,
  • Robert P. Rambo,
  • Susumu Uchiyama,
  • Kentaro Ishii,
  • Shigenori Nishimura,
  • Takashi Inui

DOI
https://doi.org/10.1038/s41467-020-15611-3
Journal volume & issue
Vol. 11, no. 1
pp. 1 – 10

Abstract

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Trypanosoma brucei guanosine 5′-monophosphate reductase (TbGMPR) catalyses the conversion of GMP to inosine 5′-monophosphate and contains a cystathionine-β-synthase (CBS) domain. Here the authors combine X-ray crystallography and kinetic measurements and present the GMP-, GTP-bound and nucleotide-free TbGMPR structures and show that guanine and adenine nucleotides are allosteric regulators of TbGMPR that bind to the CBS domain.