8YYK
Structure of RNase J2 wild type at room temperature
Summary for 8YYK
| Entry DOI | 10.2210/pdb8yyk/pdb |
| Descriptor | Ribonuclease J 2, MANGANESE (II) ION (2 entities in total) |
| Functional Keywords | ribonuclease, rnase j2, rna binding protein |
| Biological source | Staphylococcus aureus |
| Total number of polymer chains | 4 |
| Total formula weight | 257737.06 |
| Authors | |
| Primary citation | Singh, A.K.,Chinnasamy, K.,Pahelkar, N.R.,Gopal, B. A physicochemical rationale for the varied catalytic efficiency in RNase J paralogues. J.Biol.Chem., 301:108152-108152, 2024 Cited by PubMed Abstract: Paralogs of the bifunctional nuclease, Ribonuclease J (RNase J), demonstrate varied catalytic efficiencies despite extensive sequence and structural similarity. Of the two Staphylococcus aureus RNase J paralogues, RNase J1 is substantially more active than RNase J2. Mutational analysis of active site residues revealed that only H80 and E166 were critical for nuclease activity. Electronic properties of active site residues were further evaluated using density functional theory in conjunction with molecular mechanics. This analysis suggested that multiple residues at the active site can function as Lewis bases or acids in RNase J2. The bond dissociation energy, on the other hand, suggested that the Mn ion in RNase J2, located at a structurally identical location to that in RNase J1, is crucial for overall structural integrity. Structures of mutant enzymes lacking the metal ion were seen to adopt a different orientation between the substrate binding and catalytic domain than wild-type RNase J2. A surprising finding was that the RNase J2 H78 A mutant was five-fold more active than the wild-type enzyme. Structural and biochemical experiments performed in light of this observation revealed that the RNase J2 catalytic mechanism is distinct from both two-metal ion and one-metal ion reaction mechanisms proposed for RNase J nucleases. Different activity levels in RNase J paralogues can thus be ascribed to the diversity in catalytic mechanisms. PubMed: 39742998DOI: 10.1016/j.jbc.2024.108152 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
Download full validation report
