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Crystal structure of GMP reductase from Trypanosoma brucei in complex with guanosine 5'-triphosphateCrystal structure of GMP reductase from Trypanosoma brucei in complex with guanosine 5'-triphosphate
Structural highlights
FunctionPublication Abstract from PubMedGuanosine 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-beta-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. Allosteric regulation accompanied by oligomeric state changes of Trypanosoma brucei GMP reductase through cystathionine-beta-synthase domain.,Imamura A, Okada T, Mase H, Otani T, Kobayashi T, Tamura M, Kubata BK, Inoue K, Rambo RP, Uchiyama S, Ishii K, Nishimura S, Inui T Nat Commun. 2020 Apr 15;11(1):1837. doi: 10.1038/s41467-020-15611-3. PMID:32296055[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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