5OWI
The dynamic dimer structure of the chaperone Trigger Factor (conformer 1)
Summary for 5OWI
| Entry DOI | 10.2210/pdb5owi/pdb |
| NMR Information | BMRB: 27239 |
| Descriptor | Trigger factor (1 entity in total) |
| Functional Keywords | chaperone, dimer |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 96511.14 |
| Authors | Morgado, L.,Burmann, B.M.,Sharpe, T.,Mazur, A.,Hiller, S. (deposition date: 2017-09-01, release date: 2017-11-29, Last modification date: 2024-05-15) |
| Primary citation | Morgado, L.,Burmann, B.M.,Sharpe, T.,Mazur, A.,Hiller, S. The dynamic dimer structure of the chaperone Trigger Factor. Nat Commun, 8:1992-1992, 2017 Cited by PubMed Abstract: The chaperone Trigger Factor (TF) from Escherichia coli forms a dimer at cellular concentrations. While the monomer structure of TF is well known, the spatial arrangement of this dimeric chaperone storage form has remained unclear. Here, we determine its structure by a combination of high-resolution NMR spectroscopy and biophysical methods. TF forms a symmetric head-to-tail dimer, where the ribosome binding domain is in contact with the substrate binding domain, while the peptidyl-prolyl isomerase domain contributes only slightly to the dimer affinity. The dimer structure is highly dynamic, with the two ribosome binding domains populating a conformational ensemble in the center. These dynamics result from intermolecular in trans interactions of the TF client-binding site with the ribosome binding domain, which is conformationally frustrated in the absence of the ribosome. The avidity in the dimer structure explains how the dimeric state of TF can be monomerized also by weakly interacting clients. PubMed: 29222465DOI: 10.1038/s41467-017-02196-7 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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