8P37
Structure a catalytically inactive mutant of the IMP dehydrogenase related protein GUAB3 from Synechocystis PCC 6803
Summary for 8P37
| Entry DOI | 10.2210/pdb8p37/pdb |
| Descriptor | IMP dehydrogenase subunit, XANTHOSINE-5'-MONOPHOSPHATE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (4 entities in total) |
| Functional Keywords | complex of the enzyme with cofactor and product, biosynthetic protein |
| Biological source | Synechocystis sp. PCC 6803 |
| Total number of polymer chains | 1 |
| Total formula weight | 41566.44 |
| Authors | Hernandez-Gomez, A.,Fernandez-Justel, D.,Buey, R.M. (deposition date: 2023-05-17, release date: 2024-03-27) |
| Primary citation | Hernandez-Gomez, A.,Irisarri, I.,Fernandez-Justel, D.,Pelaez, R.,Jimenez, A.,Revuelta, J.L.,Balsera, M.,Buey, R.M. GuaB3, an overlooked enzyme in cyanobacteria's toolbox that sheds light on IMP dehydrogenase evolution. Structure, 31:1526-1534.e4, 2023 Cited by PubMed Abstract: IMP dehydrogenase and GMP reductase are enzymes from the same protein family with analogous structures and catalytic mechanisms that have gained attention because of their essential roles in nucleotide metabolism and as potential drug targets. This study focusses on GuaB3, a less-explored enzyme within this family. Phylogenetic analysis uncovers GuaB3's independent evolution from other members of the family and it predominantly occurs in Cyanobacteria. Within this group, GuaB3 functions as a unique IMP dehydrogenase, while its counterpart in Actinobacteria has a yet unknown function. Synechocystis sp. PCC6803 GuaB3 structures demonstrate differences in the active site compared to canonical IMP dehydrogenases, despite shared catalytic mechanisms. These findings highlight the essential role of GuaB3 in Cyanobacteria, provide insights into the diversity and evolution of the IMP dehydrogenase protein family, and reveal a distinctive characteristic in nucleotide metabolism, potentially aiding in combating harmful cyanobacterial blooms-a growing concern for humans and wildlife. PubMed: 37875114DOI: 10.1016/j.str.2023.09.014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.219 Å) |
Structure validation
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