3DYR
Crystal structure of E. coli thioredoxin mutant I76T in its oxidized form
Summary for 3DYR
| Entry DOI | 10.2210/pdb3dyr/pdb |
| Descriptor | Thioredoxin-1 (2 entities in total) |
| Functional Keywords | mutant protein, electron transport, host-virus interaction, redox-active center, transport |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 23749.08 |
| Authors | Ren, G.,Bardwell, J.C.A.,Xu, Z. (deposition date: 2008-07-28, release date: 2009-01-27, Last modification date: 2024-10-09) |
| Primary citation | Ren, G.,Stephan, D.,Xu, Z.,Zheng, Y.,Tang, D.,Harrison, R.S.,Kurz, M.,Jarrott, R.,Shouldice, S.R.,Hiniker, A.,Martin, J.L.,Heras, B.,Bardwell, J.C. Properties of the thioredoxin fold superfamily are modulated by a single amino acid residue. J.Biol.Chem., 284:10150-10159, 2009 Cited by PubMed Abstract: The ubiquitous thioredoxin fold proteins catalyze oxidation, reduction, or disulfide exchange reactions depending on their redox properties. They also play vital roles in protein folding, redox control, and disease. Here, we have shown that a single residue strongly modifies both the redox properties of thioredoxin fold proteins and their ability to interact with substrates. This residue is adjacent in three-dimensional space to the characteristic CXXC active site motif of thioredoxin fold proteins but distant in sequence. This residue is just N-terminal to the conservative cis-proline. It is isoleucine 75 in the case of thioredoxin. Our findings support the conclusion that a very small percentage of the amino acid residues of thioredoxin-related proteins are capable of dictating the functions of these proteins. PubMed: 19181668DOI: 10.1074/jbc.M809509200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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