6OAY
Structure of the hyperactive ClpB mutant K476C, bound to casein, post-state
Summary for 6OAY
| Entry DOI | 10.2210/pdb6oay/pdb |
| Related | 6OAX 6OG1 6OG2 6OG3 |
| EMDB information | 20004 20005 20049 20050 20051 |
| Descriptor | Hyperactive disaggregase ClpB, Alpha-S1-casein, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, ... (4 entities in total) |
| Functional Keywords | disaggregase, clpb, aaa+, chaperone |
| Biological source | Escherichia coli K-12 More |
| Total number of polymer chains | 7 |
| Total formula weight | 589713.09 |
| Authors | Rizo, A.R.,Lin, J.-B.,Gates, S.N.,Tse, E.,Bart, S.M.,Castellano, L.M.,Dimaio, F.,Shorter, J.,Southworth, D.R. (deposition date: 2019-03-18, release date: 2019-06-12, Last modification date: 2024-03-20) |
| Primary citation | Rizo, A.N.,Lin, J.,Gates, S.N.,Tse, E.,Bart, S.M.,Castellano, L.M.,DiMaio, F.,Shorter, J.,Southworth, D.R. Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase. Nat Commun, 10:2393-2393, 2019 Cited by PubMed Abstract: Bacterial ClpB and yeast Hsp104 are homologous Hsp100 protein disaggregases that serve critical functions in proteostasis by solubilizing protein aggregates. Two AAA+ nucleotide binding domains (NBDs) power polypeptide translocation through a central channel comprised of a hexameric spiral of protomers that contact substrate via conserved pore-loop interactions. Here we report cryo-EM structures of a hyperactive ClpB variant bound to the model substrate, casein in the presence of slowly hydrolysable ATPγS, which reveal the translocation mechanism. Distinct substrate-gripping interactions are identified for NBD1 and NBD2 pore loops. A trimer of N-terminal domains define a channel entrance that binds the polypeptide substrate adjacent to the topmost NBD1 contact. NBD conformations at the seam interface reveal how ATP hydrolysis-driven substrate disengagement and re-binding are precisely tuned to drive a directional, stepwise translocation cycle. PubMed: 31160557DOI: 10.1038/s41467-019-10150-y PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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