4D2X

Negative-stain electron microscopy of E. coli ClpB of Y503D hyperactive mutant (BAP form bound to ClpP)

Summary for 4D2X

• Entry DOI: 10.2210/pdb4d2x/pdb
• Related: 4D2Q 4D2U
• EMDB information: 2559
• Descriptor: CHAPERONE PROTEIN CLPB (1 entity in total)
• Functional Keywords: chaperone, disaggregase, clpb, bap, y503d hyperactive mutant, coiled- coil domain
• Biological source: ESCHERICHIA COLI
• 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: 2014-05-13, release date: 2014-06-04, Last modification date: 2024-10-16)

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

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: 24843029
DOI: 10.7554/ELIFE.02481

Experimental method

ELECTRON MICROSCOPY (20 Å)