1V9Q
Crystal Structure of an Artificial Metalloprotein:Mn(III)(3,3'-Me2-salophen)/apo-A71G Myoglobin
Summary for 1V9Q
| Entry DOI | 10.2210/pdb1v9q/pdb |
| Related | 1J3F |
| Descriptor | Myoglobin, PHOSPHATE ION, 'N,N'-BIS-(2-HYDROXY-3-METHYL-BENZYLIDENE)-BENZENE-1,2-DIAMINE', ... (5 entities in total) |
| Functional Keywords | myoglobin, schiff base, manganese, salophen, metalloprotein, oxygen storage-transport complex, oxygen storage/transport |
| Biological source | Physeter catodon (sperm whale) |
| Total number of polymer chains | 1 |
| Total formula weight | 18321.29 |
| Authors | Ueno, T.,Koshiyama, T.,Kono, M.,Kondo, K.,Ohashi, M.,Suzuki, A.,Yamane, T.,Watanabe, Y. (deposition date: 2004-01-29, release date: 2005-05-17, Last modification date: 2023-10-25) |
| Primary citation | Ueno, T.,Koshiyama, T.,Ohashi, M.,Kondo, K.,Kono, M.,Suzuki, A.,Yamane, T.,Watanabe, Y. Coordinated Design of Cofactor and Active Site Structures in Development of New Protein Catalysts J.Am.Chem.Soc., 127:6556-6562, 2005 Cited by PubMed Abstract: New methods for the synthesis of artificial metalloenzymes are important for the construction of novel biocatalysts and biomaterials. Recently, we reported new methodology for the synthesis of artificial metalloenzymes by reconstituting apo-myoglobin with metal complexes (Ohashi, M. et al., Angew Chem., Int. Ed. 2003, 42, 1005-1008). However, it has been difficult to improve their reactivity, since their crystal structures were not available. In this article, we report the crystal structures of M(III)(Schiff base).apo-A71GMbs (M = Cr and Mn). The structures suggest that the position of the metal complex in apo-Mb is regulated by (i) noncovalent interaction between the ligand and surrounding peptides and (ii) the ligation of the metal ion to proximal histidine (His93). In addition, it is proposed that specific interactions of Ile107 with 3- and 3'-substituent groups on the salen ligand control the location of the Schiff base ligand in the active site. On the basis of these results, we have successfully controlled the enantioselectivity in the sulfoxidation of thioanisole by changing the size of substituents at the 3 and 3' positions. This is the first example of an enantioselective enzymatic reaction regulated by the design of metal complex in the protein active site. PubMed: 15869276DOI: 10.1021/ja045995q PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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