5O6G
Structures and dynamics of mesophilic variants from the homing endonuclease I-DmoI
Summary for 5O6G
| Entry DOI | 10.2210/pdb5o6g/pdb |
| Related | 5o6g |
| Descriptor | Homing endonuclease I-DmoI, DNA (25-MER), MANGANESE (II) ION, ... (6 entities in total) |
| Functional Keywords | desulfurococcus mobilis, dna binding protein |
| Biological source | Desulfurococcus mucosus More |
| Total number of polymer chains | 9 |
| Total formula weight | 116789.38 |
| Authors | Molina, R.,Marcaida, M.J. (deposition date: 2017-06-06, release date: 2017-12-06, Last modification date: 2024-01-17) |
| Primary citation | Alba, J.,Marcaida, M.J.,Prieto, J.,Montoya, G.,Molina, R.,D'Abramo, M. Structure and dynamics of mesophilic variants from the homing endonuclease I-DmoI. J. Comput. Aided Mol. Des., 31:1063-1072, 2017 Cited by PubMed Abstract: I-DmoI, from the hyperthermophilic archaeon Desulfurococcus mobilis, belongs to the LAGLIDADG homing endonuclease protein family. Its members are highly specific enzymes capable of recognizing long DNA target sequences, thus providing potential tools for genome manipulation. Working towards this particular application, many efforts have been made to generate mesophilic variants of I-DmoI that function at lower temperatures than the wild-type. Here, we report a structural and computational analysis of two I-DmoI mesophilic mutants. Despite very limited structural variations between the crystal structures of these variants and the wild-type, a different dynamical behaviour near the cleavage sites is observed. In particular, both the dynamics of the water molecules and the protein perturbation effect on the cleavage site correlate well with the changes observed in the experimental enzymatic activity. PubMed: 29177929DOI: 10.1007/s10822-017-0087-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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