5OJB
Structure of MbQ NMH
Summary for 5OJB
| Entry DOI | 10.2210/pdb5ojb/pdb |
| Descriptor | Myoglobin, PROTOPORPHYRIN IX CONTAINING FE, IMIDAZOLE, ... (4 entities in total) |
| Functional Keywords | myoglobin, nmh, n-methylhistidine, heme, oxidoreductase |
| Biological source | Physeter catodon (Sperm whale) |
| Total number of polymer chains | 1 |
| Total formula weight | 19064.75 |
| Authors | Hayashi, T.,Pott, M.,Mori, T.,Mittl, P.,Green, A.,Hivert, D. (deposition date: 2017-07-21, release date: 2018-01-24, Last modification date: 2024-01-17) |
| Primary citation | Pott, M.,Hayashi, T.,Mori, T.,Mittl, P.R.E.,Green, A.P.,Hilvert, D. A Noncanonical Proximal Heme Ligand Affords an Efficient Peroxidase in a Globin Fold. J. Am. Chem. Soc., 140:1535-1543, 2018 Cited by PubMed Abstract: Expanding the range of genetically encoded metal coordination environments accessible within tunable protein scaffolds presents excellent opportunities for the creation of metalloenzymes with augmented properties and novel activities. Here, we demonstrate that installation of a noncanonical N-methyl histidine (NMH) as the proximal heme ligand in the oxygen binding protein myoglobin (Mb) leads to substantial increases in heme redox potential and promiscuous peroxidase activity. Structural characterization of this catalytically modified myoglobin variant (Mb NMH) revealed significant changes in the proximal pocket, including alterations to hydrogen-bonding interactions involving the prosthetic porphyrin cofactor. Further optimization of Mb NMH via a combination of rational modification and several rounds of laboratory evolution afforded efficient peroxidase biocatalysts within a globin fold, with activities comparable to those displayed by nature's peroxidases. PubMed: 29309143DOI: 10.1021/jacs.7b12621 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.543 Å) |
Structure validation
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