Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation.
Journal, issue, pages	Elife, Vol. 3, Page e02481, Year 2014
Publish date	Apr 30, 2014
Authors	Marta Carroni / Eva Kummer / Yuki Oguchi / Petra Wendler / Daniel K Clare / Irmgard Sinning / Jürgen Kopp / Axel Mogk / Bernd Bukau / Helen R Saibil /
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 ...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.
External links	Elife / PubMed:24843029 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	3.5 - 29.0 Å
Structure data	2555 4d2q EMDB-2555, PDB-4d2q: Negative-stain electron microscopy of E. coli ClpB mutant E432A (BAP form bound to ClpP) Method: EM (single particle) / Resolution: 18.0 Å EMDB-2556: Negative-stain electron microscopy of E. coli ClpB mutant E432A (BAP form bound to ClpP) Method: EM (single particle) / Resolution: 21.0 Å 2557 4d2u EMDB-2557, PDB-4d2u: Negative-stain electron microscopy of E. coli ClpB (BAP form bound to ClpP) Method: EM (single particle) / Resolution: 17.0 Å EMDB-2558: Negative-stain electron microscopy of E. coli ClpB (BAP form bound to ClpP) Method: EM (single particle) / Resolution: 21.0 Å 2559 4d2x EMDB-2559: Negative-stain electron microscopy of E. coli ClpB (BAP form bound to ClpP) PDB-4d2x: Negative-stain electron microscopy of E. coli ClpB of Y503D hyperactive mutant (BAP form bound to ClpP) Method: EM (single particle) / Resolution: 20.0 Å EMDB-2560: Negative-stain electron microscopy of E. coli ClpB (BAP form bound to ClpP) Method: EM (single particle) / Resolution: 25.0 Å EMDB-2561: Negative-stain electron microscopy of Hsp104 (HAP form bound to ClpP) Method: EM (single particle) / Resolution: 21.0 Å EMDB-2562: Cryo electron microscopy of E. coli ClpB DWB mutant (BAP form bound to ClpP) Method: EM (single particle) / Resolution: 24.0 Å EMDB-2563: Cryo electron microscopy of E. coli ClpB Method: EM (single particle) / Resolution: 29.0 Å PDB-4ciu: Crystal structure of E. coli ClpB Method: X-RAY DIFFRACTION / Resolution: 3.5 Å
Chemicals	ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate
Source	escherichia coli (E. coli) Saccharomyces cerevisiae (brewer's yeast)
Keywords	CHAPERONE / AAA+ / ATPASE / DISAGGREGASE / CLPB / BAP / COILED-COIL DOMAIN / WILD TYPE / Y503D HYPERACTIVE MUTANT / COILED- COIL DOMAIN