4FCV

Crystal structure of the C-terminal domain of ClpB

Summary for 4FCV

• Entry DOI: 10.2210/pdb4fcv/pdb
• Related: 4FCT 4FCW 4FD2
• Descriptor: Chaperone protein ClpB, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
• Functional Keywords: aaa domain, chaperone
• Biological source: Thermus thermophilus
• Cellular location: Cytoplasm (Probable): Q9RA63
• Total number of polymer chains: 3
• Total formula weight: 108126.63

Authors

Biter, A.B.,Lee, S.,Sung, N.,Tsai, F.T.F. (deposition date: 2012-05-25, release date: 2012-07-18, Last modification date: 2024-10-30)

Primary citation

Biter, A.B.,Lee, S.,Sung, N.,Tsai, F.T.
Structural basis for intersubunit signaling in a protein disaggregating machine.
Proc.Natl.Acad.Sci.USA, 109:12515-12520, 2012

PubMed Abstract: ClpB is a ring-forming, ATP-dependent protein disaggregase that cooperates with the cognate Hsp70 system to recover functional protein from aggregates. How ClpB harnesses the energy of ATP binding and hydrolysis to facilitate the mechanical unfolding of previously aggregated, stress-damaged proteins remains unclear. Here, we present crystal structures of the ClpB D2 domain in the nucleotide-bound and -free states, and the fitted cryoEM structure of the D2 hexamer ring, which provide a structural understanding of the ATP power stroke that drives protein translocation through the ClpB hexamer. We demonstrate that the conformation of the substrate-translocating pore loop is coupled to the nucleotide state of the cis subunit, which is transmitted to the neighboring subunit via a conserved but structurally distinct intersubunit-signaling pathway common to diverse AAA+ machines. Furthermore, we found that an engineered, disulfide cross-linked ClpB hexamer is fully functional biochemically, suggesting that ClpB deoligomerization is not required for protein disaggregation.

PubMed: 22802670
DOI: 10.1073/pnas.1207040109

Experimental method

X-RAY DIFFRACTION (3.4 Å)