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| Title | Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB. |
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| Journal, issue, pages | Mol Cell, Vol. 25, Issue 2, Page 261-271, Year 2007 |
| Publish date | Jan 26, 2007 |
 Authors | Sukyeong Lee / Jae-Mun Choi / Francis T F Tsai /  |
| PubMed Abstract | ClpB is a ring-shaped molecular chaperone that has the remarkable ability to disaggregate stress-damaged proteins. Here we present the electron cryomicroscopy reconstruction of an ATP-activated ClpB ...ClpB is a ring-shaped molecular chaperone that has the remarkable ability to disaggregate stress-damaged proteins. Here we present the electron cryomicroscopy reconstruction of an ATP-activated ClpB trap mutant, along with reconstructions of ClpB in the AMPPNP, ADP, and in the nucleotide-free state. We show that motif 2 of the ClpB M domain is positioned between the D1-large domains of neighboring subunits and could facilitate a concerted, ATP-driven conformational change in the AAA-1 ring. We further demonstrate biochemically that ATP is essential for high-affinity substrate binding to ClpB and cannot be substituted with AMPPNP. Our structures show that in the ATP-activated state, the D1 loops are stabilized at the central pore, providing the structural basis for high-affinity substrate binding. Taken together, our results support a mechanism by which ClpB captures substrates on the upper surface of the AAA-1 ring before threading them through the ClpB hexamer in an ATP hydrolysis-driven step. |
 External links | Mol Cell / PubMed:17244533 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 11.2 - 17.7 Å |
| Structure data |  EMDB-1241:  EMDB-1242:  EMDB-1243:  EMDB-1244: |
| Source |
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Thermus thermophilus (bacteria)