1XTL
Crystal structure of P104H mutant of SOD-like protein from Bacillus subtilis.
Summary for 1XTL
| Entry DOI | 10.2210/pdb1xtl/pdb |
| Related | 1S4I 1XTM |
| Descriptor | Hypothetical superoxide dismutase-like protein yojM, COPPER (II) ION, ZINC ION, ... (4 entities in total) |
| Functional Keywords | sod, cu-zn sod, sod-like, superoxide dismutase mutants, structural genomics, unknown function |
| Biological source | Bacillus subtilis |
| Cellular location | Cell membrane; Lipid-anchor (Potential): O31851 |
| Total number of polymer chains | 4 |
| Total formula weight | 76027.57 |
| Authors | Calderone, V.,Mangani, S.,Banci, L.,Benvenuti, M.,Bertini, I.,Viezzoli, M.S.,Fantoni, A. (deposition date: 2004-10-22, release date: 2005-10-04, Last modification date: 2024-10-23) |
| Primary citation | Banci, L.,Benvenuti, M.,Bertini, I.,Cabelli, D.E.,Calderone, V.,Fantoni, A.,Mangani, S.,Migliardi, M.,Viezzoli, M.S. From an Inactive Prokaryotic SOD Homologue to an Active Protein through Site-Directed Mutagenesis. J.Am.Chem.Soc., 127:13287-13292, 2005 Cited by PubMed Abstract: It is known that several prokaryotic protein sequences, characterized by high homology with the eukaryotic Cu,ZnSODs, lack some of the metal ligands. In the present work, we have stepwise reintroduced the two missing copper ligands in the SOD-like protein of Bacillus subtilis, through site-directed mutagenesis. The mutant with three out of the four His that bind copper is not active, whereas the fully reconstituted mutant displays an activity of about 10% that of human Cu,ZnSOD. The mutated proteins have been characterized in solution and in the solid state. In solution, the proteins experience conformational disorder, which is believed to be partly responsible for the decreased enzymatic activity and sheds light on the tendency of several human SOD mutants to introduce mobility in the protein frame. In the crystal, on the contrary, the protein has a well-defined conformation, giving rise to dimers through the coordination of an exogenous zinc ion. The catalytic properties of the double mutant, which might be regarded as a step in an artificial evolution from a nonactive SOD to a fully functioning enzyme, are discussed on the basis of the structural and dynamical properties. PubMed: 16173759DOI: 10.1021/ja052790o PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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