4WR5
Crystal Structure of GST Mutated with Halogenated Tyrosine (7cGST-1)
Summary for 4WR5
| Entry DOI | 10.2210/pdb4wr5/pdb |
| Related | 4WR4 |
| Descriptor | Glutathione S-transferase class-mu 26 kDa isozyme, GLUTATHIONE, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | themostabilized structure, homodimeric, two domains, alfa/beta, alfa, detoxification, xenobiotic compounds, gutathione, 7 specfic sites, cytoplasmic, transferase |
| Biological source | Schistosoma japonicum (Blood fluke) |
| Total number of polymer chains | 1 |
| Total formula weight | 28876.05 |
| Authors | Akasaka, R.,Kawazoe, M.,Tomabechi, Y.,Ohtake, K.,Itagaki, T.,Takemoto, C.,Shirouzu, M.,Yokoyama, S.,Sakamoto, K. (deposition date: 2014-10-23, release date: 2015-08-19, Last modification date: 2023-11-08) |
| Primary citation | Ohtake, K.,Yamaguchi, A.,Mukai, T.,Kashimura, H.,Hirano, N.,Haruki, M.,Kohashi, S.,Yamagishi, K.,Murayama, K.,Tomabechi, Y.,Itagaki, T.,Akasaka, R.,Kawazoe, M.,Takemoto, C.,Shirouzu, M.,Yokoyama, S.,Sakamoto, K. Protein stabilization utilizing a redefined codon Sci Rep, 5:9762-9762, 2015 Cited by PubMed Abstract: Recent advances have fundamentally changed the ways in which synthetic amino acids are incorporated into proteins, enabling their efficient and multiple-site incorporation, in addition to the 20 canonical amino acids. This development provides opportunities for fresh approaches toward addressing fundamental problems in bioengineering. In the present study, we showed that the structural stability of proteins can be enhanced by integrating bulky halogenated amino acids at multiple selected sites. Glutathione S-transferase was thus stabilized significantly (by 5.2 and 5.6 kcal/mol) with 3-chloro- and 3-bromo-l-tyrosines, respectively, incorporated at seven selected sites. X-ray crystallographic analyses revealed that the bulky halogen moieties filled internal spaces within the molecules, and formed non-canonical stabilizing interactions with the neighboring residues. This new mechanism for protein stabilization is quite simple and applicable to a wide range of proteins, as demonstrated by the rapid stabilization of the industrially relevant azoreductase. PubMed: 25985257DOI: 10.1038/srep09762 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.93 Å) |
Structure validation
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