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 and Takashi Inui ()
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Akira Imamura: Osaka Prefecture University
Tetsuya Okada: Osaka Prefecture University
Hikaru Mase: Osaka Prefecture University
Takuya Otani: Osaka Prefecture University
Tomoka Kobayashi: Osaka Prefecture University
Manatsu Tamura: Osaka Prefecture University
Bruno Kilunga Kubata: AU/NEPAD Agency Regional Office for Eastern and Central Africa
Katsuaki Inoue: Diamond Light Source
Robert P. Rambo: Diamond Light Source
Susumu Uchiyama: Osaka University
Kentaro Ishii: National Institutes of Natural Sciences
Shigenori Nishimura: Osaka Prefecture University
Takashi Inui: Osaka Prefecture University

Nature Communications, 2020, vol. 11, issue 1, 1-10

Abstract: Abstract Guanosine 5′-monophosphate reductase (GMPR) is involved in the purine salvage pathway and is conserved throughout evolution. Nonetheless, the GMPR of Trypanosoma brucei (TbGMPR) includes a unique structure known as the cystathionine-β-synthase (CBS) domain, though the role of this domain is not fully understood. Here, we show that guanine and adenine nucleotides exert positive and negative effects, respectively, on TbGMPR activity by binding allosterically to the CBS domain. The present structural analyses revealed that TbGMPR forms an octamer that shows a transition between relaxed and twisted conformations in the absence and presence of guanine nucleotides, respectively, whereas the TbGMPR octamer dissociates into two tetramers when ATP is available instead of guanine nucleotides. These findings demonstrate that the CBS domain plays a key role in the allosteric regulation of TbGMPR by facilitating the transition of its oligomeric state depending on ligand nucleotide availability.

Date: 2020
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-15611-3

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DOI: 10.1038/s41467-020-15611-3

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