5M6S
folding intermediate of spectrin R16
Summary for 5M6S
| Entry DOI | 10.2210/pdb5m6s/pdb |
| EMDB information | 3451 |
| Descriptor | spectrin (1 entity in total) |
| Functional Keywords | spectrin, r16, structural protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 19370.60 |
| Authors | Nilsson, O.B.,Nickson, A.A.,Clarke, J. (deposition date: 2016-10-25, release date: 2017-01-11, Last modification date: 2024-05-08) |
| Primary citation | Nilsson, O.B.,Nickson, A.A.,Hollins, J.J.,Wickles, S.,Steward, A.,Beckmann, R.,von Heijne, G.,Clarke, J. Cotranslational folding of spectrin domains via partially structured states. Nat. Struct. Mol. Biol., 24:221-225, 2017 Cited by PubMed Abstract: How do the key features of protein folding, elucidated from studies on native, isolated proteins, manifest in cotranslational folding on the ribosome? Using a well-characterized family of homologous α-helical proteins with a range of biophysical properties, we show that spectrin domains can fold vectorially on the ribosome and may do so via a pathway different from that of the isolated domain. We use cryo-EM to reveal a folded or partially folded structure, formed in the vestibule of the ribosome. Our results reveal that it is not possible to predict which domains will fold within the ribosome on the basis of the folding behavior of isolated domains; instead, we propose that a complex balance of the rate of folding, the rate of translation and the lifetime of folded or partly folded states will determine whether folding occurs cotranslationally on actively translating ribosomes. PubMed: 28112730DOI: 10.1038/nsmb.3355 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.8 Å) |
Structure validation
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