PDBsum entry 4d2u

Chaperone

PDB id: 4d2u

Contents

Protein chains

(+ 0 more) 789 a.a.

PDB id:

4d2u

Name:

Chaperone

Title:

Negative-stain electron microscopy of e. Coli clpb (bap form bound to clpp)

Structure:

Chaperone protein clpb. Chain: a, b, c, d, e, f. Synonym: clpb, heat shock protein f84.1. Engineered: yes. Other_details: the protein is engineered to bind to clpp.

Source:

Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.

Authors:

M.Carroni,E.Kummer,Y.Oguchi,D.K.Clare,P.Wendler,I.Sinning,J.Kopp, A.Mogk,B.Bukau,H.R.Saibil

Key ref:

M.Carroni et al. (2014). Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation. Elife, 3, e02481. PubMed id: 24843029

Date:

13-May-14 Release date: 04-Jun-14

Protein chains

P63284  (CLPB_ECOLI) -  Chaperone protein ClpB from Escherichia coli (strain K12)

Seq: 857 a.a.

Struc: 789 a.a.

Elife 3:e02481 (2014)

PubMed id: 24843029

Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation.

M.Carroni, E.Kummer, Y.Oguchi, P.Wendler, D.K.Clare, I.Sinning, J.Kopp, A.Mogk, B.Bukau, H.R.Saibil.

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.