4TM7
Crystal structure of 6-phosphogluconolactonase from Mycobacterium smegmatis N131D mutant soaked with CuSO4
Summary for 4TM7
| Entry DOI | 10.2210/pdb4tm7/pdb |
| Related | 4TM8 |
| Descriptor | 6-phosphogluconolactonase, 1,2-ETHANEDIOL, SULFATE ION, ... (7 entities in total) |
| Functional Keywords | rossmann fold, hydrolase |
| Biological source | Mycobacterium smegmatis |
| Total number of polymer chains | 1 |
| Total formula weight | 28313.82 |
| Authors | Fujieda, N.,Stuttfeld, E.,Maier, T. (deposition date: 2014-05-31, release date: 2015-06-03, Last modification date: 2024-03-20) |
| Primary citation | Fujieda, N.,Schatti, J.,Stuttfeld, E.,Ohkubo, K.,Maier, T.,Fukuzumi, S.,Ward, T.R. Enzyme repurposing of a hydrolase as an emergent peroxidase upon metal binding. Chem Sci, 6:4060-4065, 2015 Cited by PubMed Abstract: As an alternative to Darwinian evolution relying on catalytic promiscuity, a protein may acquire auxiliary function upon metal binding, thus providing it with a novel catalytic machinery. Here we show that addition of cupric ions to a 6-phosphogluconolactonase bearing a putative metal binding site leads to the emergence of peroxidase activity ( 7.8 × 10 s, 1.1 × 10 M). Both X-ray crystallographic and EPR data of the copper-loaded enzyme reveal a bis-histidine coordination site, located within a shallow binding pocket capable of accommodating the -dianisidine substrate. PubMed: 29218172DOI: 10.1039/c5sc01065a PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.39 Å) |
Structure validation
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