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	Two-Step Activation Mechanism of the ClpB Disaggregase for Sequential Substrate Threading by the Main ATPase Motor.
Journal, issue, pages	Cell Rep, Vol. 27, Issue 12, Page 3433-33446.e4, Year 2019
Publish date	Jun 18, 2019
Authors	Célia Deville / Kamila Franke / Axel Mogk / Bernd Bukau / Helen R Saibil /
PubMed Abstract	AAA+ proteins form asymmetric hexameric rings that hydrolyze ATP and thread substrate proteins through a central channel via mobile substrate-binding pore loops. Understanding how ATPase and ...AAA+ proteins form asymmetric hexameric rings that hydrolyze ATP and thread substrate proteins through a central channel via mobile substrate-binding pore loops. Understanding how ATPase and threading activities are regulated and intertwined is key to understanding the AAA+ protein mechanism. We studied the disaggregase ClpB, which contains tandem ATPase domains (AAA1, AAA2) and shifts between low and high ATPase and threading activities. Coiled-coil M-domains repress ClpB activity by encircling the AAA1 ring. Here, we determine the mechanism of ClpB activation by comparing ATPase mechanisms and cryo-EM structures of ClpB wild-type and a constitutively active ClpB M-domain mutant. We show that ClpB activation reduces ATPase cooperativity and induces a sequential mode of ATP hydrolysis in the AAA2 ring, the main ATPase motor. AAA1 and AAA2 rings do not work synchronously but in alternating cycles. This ensures high grip, enabling substrate threading via a processive, rope-climbing mechanism.
External links	Cell Rep / PubMed:31216466 / PubMed Central
Methods	EM (single particle)
Resolution	3.4 - 6.2 Å
Structure data	4621 6qs4 EMDB-4621, PDB-6qs4: Two-Step Activation Mechanism of the ClpB Disaggregase for Sequential Substrate Threading by the Main ATPase Motor. Method: EM (single particle) / Resolution: 4.2 Å EMDB-4622: E. coli ClpB (DWB and K476C mutant) bound to casein - middle domain conformation 1 Method: EM (single particle) / Resolution: 3.7 Å EMDB-4623: E. coli ClpB (DWB and K476C mutant) bound to casein - middle domain conformation 2 Method: EM (single particle) / Resolution: 3.8 Å 4624 6qs6 EMDB-4624, PDB-6qs6: ClpB (DWB and K476C mutant) bound to casein in presence of ATPgammaS - state KC-1 Method: EM (single particle) / Resolution: 3.9 Å EMDB-4625: E. coli ClpB (DWB and K476C mutant) bound to casein - state KC-2 Method: EM (single particle) / Resolution: 3.4 Å 4626 6qs7 EMDB-4626, PDB-6qs7: ClpB (DWB and K476C mutant) bound to casein in presence of ATPgammaS - state KC-2A Method: EM (single particle) / Resolution: 3.8 Å 4627 6qs8 EMDB-4627, PDB-6qs8: ClpB (DWB and K476C mutant) bound to casein in presence of ATPgammaS - state KC-2B Method: EM (single particle) / Resolution: 3.9 Å 4940 6rn2 EMDB-4940, PDB-6rn2: ClpB (DWB mutant) bound to casein in presence of ATPgammaS - state WT-1 Method: EM (single particle) / Resolution: 6.2 Å 4941 6rn3 EMDB-4941, PDB-6rn3: ClpB (DWB mutant) bound to casein in presence of ATPgammaS - state WT-2A Method: EM (single particle) / Resolution: 4.0 Å 4942 6rn4 EMDB-4942, PDB-6rn4: ClpB (DWB mutant) bound to casein in presence of ATPgammaS - state WT-2B Method: EM (single particle) / Resolution: 4.2 Å
Chemicals	ChemComp-AGS: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogueYM ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM / Adenosine diphosphate ChemComp-MG: Unknown entry
Source	escherichia coli (E. coli) escherichia coli (strain atcc 9637 / ccm 2024 / dsm 1116 / ncimb 8666 / nrrl b-766 / w) (bacteria) bos taurus (cattle) escherichia coli hvh 50 (4-2593475) (bacteria)
Keywords	CHAPERONE / disaggregase / proteostasis / AAA