3T2X
Structure of shwanavidin low affinity mutant (F43A)
Summary for 3T2X
| Entry DOI | 10.2210/pdb3t2x/pdb |
| Related | 3SZH 3szi 3szj 3t2w |
| Descriptor | Avidin/streptavidin (2 entities in total) |
| Functional Keywords | avidin, biotin, streptavidin, shwanavidin, high affinity systems, biotin-binding protein |
| Biological source | Shewanella denitrificans |
| Total number of polymer chains | 4 |
| Total formula weight | 51841.12 |
| Authors | Livnah, O.,Meir, A. (deposition date: 2011-07-23, release date: 2012-04-11, Last modification date: 2024-11-06) |
| Primary citation | Meir, A.,Bayer, E.A.,Livnah, O. Structural Adaptation of a Thermostable Biotin-binding Protein in a Psychrophilic Environment. J.Biol.Chem., 287:17951-17962, 2012 Cited by PubMed Abstract: Shwanavidin is an avidin-like protein from the marine proteobactrium Shewanella denitrificans, which exhibits an innate dimeric structure while maintaining high affinity toward biotin. A unique residue (Phe-43) from the L3,4 loop and a distinctive disulfide bridge were shown to account for the high affinity toward biotin. Phe-43 emulates the function and position of the critical intermonomeric Trp that characterizes the tetrameric avidins but is lacking in shwanavidin. The 18 copies of the apo-monomer revealed distinctive snapshots of L3,4 and Phe-43, providing rare insight into loop flexibility, binding site accessibility, and psychrophilic adaptation. Nevertheless, as in all avidins, shwanavidin also displays high thermostability properties. The unique features of shwanavidin may provide a platform for the design of a long sought after monovalent form of avidin, which would be ideal for novel types of biotechnological application. PubMed: 22493427DOI: 10.1074/jbc.M112.357186 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.15 Å) |
Structure validation
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