5CEG
X-ray structure of toxin/anti-toxin complex from Mesorhizobium opportunistum
Summary for 5CEG
| Entry DOI | 10.2210/pdb5ceg/pdb |
| Descriptor | Addiction module antidote protein, CopG/Arc/MetJ family, Plasmid stabilization system, GLYCEROL, ... (6 entities in total) |
| Functional Keywords | toxin anti-toxin, toxin |
| Biological source | Mesorhizobium opportunistum (strain LMG 24607 / HAMBI 3007 / WSM2075) More |
| Total number of polymer chains | 4 |
| Total formula weight | 49895.56 |
| Authors | Aakre, C.D.,Herrou, J.,Crosson, S.,Laub, M.T. (deposition date: 2015-07-06, release date: 2015-11-11, Last modification date: 2024-03-06) |
| Primary citation | Aakre, C.D.,Herrou, J.,Phung, T.N.,Perchuk, B.S.,Crosson, S.,Laub, M.T. Evolving New Protein-Protein Interaction Specificity through Promiscuous Intermediates. Cell, 163:594-606, 2015 Cited by PubMed Abstract: Interacting proteins typically coevolve, and the identification of coevolving amino acids can pinpoint residues required for interaction specificity. This approach often assumes that an interface-disrupting mutation in one protein drives selection of a compensatory mutation in its partner during evolution. However, this model requires a non-functional intermediate state prior to the compensatory change. Alternatively, a mutation in one protein could first broaden its specificity, allowing changes in its partner, followed by a specificity-restricting mutation. Using bacterial toxin-antitoxin systems, we demonstrate the plausibility of this second, promiscuity-based model. By screening large libraries of interface mutants, we show that toxins and antitoxins with high specificity are frequently connected in sequence space to more promiscuous variants that can serve as intermediates during a reprogramming of interaction specificity. We propose that the abundance of promiscuous variants promotes the expansion and diversification of toxin-antitoxin systems and other paralogous protein families during evolution. PubMed: 26478181DOI: 10.1016/j.cell.2015.09.055 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.59 Å) |
Structure validation
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