6jl8

Crystal structure of GMP reductase C318A from Trypanosoma brucei

spinqualitylabelsall models 6jl8, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6jl8 is a 2 chain structure with sequence from Trypanosoma brucei brucei. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.804Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q57ZS7_TRYB2 Publication Abstract from PubMed 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-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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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