6S36
Crystal structure of E. coli Adenylate kinase R119K mutant
Summary for 6S36
| Entry DOI | 10.2210/pdb6s36/pdb |
| Descriptor | Adenylate kinase, CHLORIDE ION, SODIUM ION, ... (5 entities in total) |
| Functional Keywords | adenylate kinase, r119k variant, transferase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 23769.98 |
| Authors | Grundstrom, C.,Rogne, P.,Wolf-Watz, M.,Sauer-Eriksson, A.E. (deposition date: 2019-06-24, release date: 2019-08-07, Last modification date: 2024-01-24) |
| Primary citation | Rogne, P.,Andersson, D.,Grundstrom, C.,Sauer-Eriksson, E.,Linusson, A.,Wolf-Watz, M. Nucleation of an Activating Conformational Change by a Cation-pi Interaction. Biochemistry, 58:3408-3412, 2019 Cited by PubMed Abstract: As a key molecule in biology, adenosine triphosphate (ATP) has numerous crucial functions in, for instance, energetics, post-translational modifications, nucleotide biosynthesis, and cofactor metabolism. Here, we have discovered an intricate interplay between the enzyme adenylate kinase and its substrate ATP. The side chain of an arginine residue was found to be an efficient sensor of the aromatic moiety of ATP through the formation of a strong cation-π interaction. In addition to recognition, the interaction was found to have dual functionality. First, it nucleates the activating conformational transition of the ATP binding domain and also affects the specificity in the distant AMP binding domain. In light of the functional consequences resulting from the cation-π interaction, it is possible that the mode of ATP recognition may be a useful tool in enzyme design. PubMed: 31339702DOI: 10.1021/acs.biochem.9b00538 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
Download full validation report
