4D2Q
Negative-stain electron microscopy of E. coli ClpB mutant E432A (BAP form bound to ClpP)
Summary for 4D2Q
Entry DOI | 10.2210/pdb4d2q/pdb |
Related | 4D2U 4D2X |
EMDB information | 2555 |
Descriptor | CLPB (1 entity in total) |
Functional Keywords | chaperone, disaggregase, clpb, bap, coiled-coil domain |
Biological source | ESCHERICHIA COLI |
Cellular location | Cytoplasm : P63284 |
Total number of polymer chains | 6 |
Total formula weight | 581010.52 |
Authors | Carroni, M.,Kummer, E.,Oguchi, Y.,Clare, D.K.,Wendler, P.,Sinning, I.,Kopp, J.,Mogk, A.,Bukau, B.,Saibil, H.R. (deposition date: 2014-05-12, release date: 2014-06-04, Last modification date: 2017-08-23) |
Primary citation | Carroni, M.,Kummer, E.,Oguchi, Y.,Wendler, P.,Clare, D.K.,Sinning, I.,Kopp, J.,Mogk, A.,Bukau, B.,Saibil, H.R. Head-to-Tail Interactions of the Coiled-Coil Domains Regulate Clpb Activity and Cooperation with Hsp70 in Protein Disaggregation. Elife, 3:02481-, 2014 Cited by PubMed Abstract: The hexameric AAA+ chaperone ClpB reactivates aggregated proteins in cooperation with the Hsp70 system. Essential for disaggregation, the ClpB middle domain (MD) is a coiled-coil propeller that binds Hsp70. Although the ClpB subunit structure is known, positioning of the MD in the hexamer and its mechanism of action are unclear. We obtained electron microscopy (EM) structures of the BAP variant of ClpB that binds the protease ClpP, clearly revealing MD density on the surface of the ClpB ring. Mutant analysis and asymmetric reconstructions show that MDs adopt diverse positions in a single ClpB hexamer. Adjacent, horizontally oriented MDs form head-to-tail contacts and repress ClpB activity by preventing Hsp70 interaction. Tilting of the MD breaks this contact, allowing Hsp70 binding, and releasing the contact in adjacent subunits. Our data suggest a wavelike activation of ClpB subunits around the ring.DOI: http://dx.doi.org/10.7554/eLife.02481.001. PubMed: 24843029DOI: 10.7554/ELIFE.02481 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (18 Å) |
Structure validation
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