1UFJ
Crystal Structure of an Artificial Metalloprotein:Fe(III)(3,3'-Me2-salophen)/apo-A71G Myoglobin
Summary for 1UFJ
| Entry DOI | 10.2210/pdb1ufj/pdb |
| Descriptor | MYOGLOBIN, FE (III) ION, PHOSPHATE ION, ... (5 entities in total) |
| Functional Keywords | myoglobin, schiff base, iron, salophen, metalloprotein, oxygen storage-transport complex, oxygen storage/transport |
| Biological source | Physeter catodon (sperm whale) |
| Total number of polymer chains | 1 |
| Total formula weight | 18322.20 |
| Authors | Ueno, T.,Ohashi, M.,Kono, M.,Kondo, K.,Suzuki, A.,Yamane, T.,Watanabe, Y. (deposition date: 2003-05-30, release date: 2004-05-18, Last modification date: 2023-10-25) |
| Primary citation | Ueno, T.,Ohashi, M.,Kono, M.,Kondo, K.,Suzuki, A.,Yamane, T.,Watanabe, Y. Crystal Structures of Artificial Metalloproteins: Tight Binding of Fe(III)(Schiff-Base) by Mutation of Ala71 to Gly in Apo-Myoglobin Inorg.Chem., 43:2852-2858, 2004 Cited by PubMed Abstract: Apo-myoglobin (apo-Mb) and apo-A71GMb were successfully reconstituted with FeIII(salophen) (1) (salophen = N,N'-bis(salicylidene)-1,2-phenilenediamine), Fe(III)(3,3'-Me2-salophen) (2), and FeIII(5,5'-t-Bu2-salophen) (3). The crystal structure of 2.apo-A71GMb shows the tight binding of the complex in the Mb cavity, while in wild-type apo-Mb it is highly disordered due to the steric repulsion with Ala71. Furthermore, the structure of 2.apo-A71GMb suggests a possible accommodation of a small substrate in the cavity. In fact, the cyanide association rate constant of 2.apo-A71GMb is 216-fold larger compared to that of 2.apo-Mb. These results provide us principles for the noncovalent fixation of synthetic metal cofactors at the desired positions in protein matrixes. PubMed: 15106972DOI: 10.1021/ic0498539 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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