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TitleTwo-Step Activation Mechanism of the ClpB Disaggregase for Sequential Substrate Threading by the Main ATPase Motor.
Journal, issue, pagesCell Rep, Vol. 27, Issue 12, Page 3433-33446.e4, Year 2019
Publish dateJun 18, 2019
AuthorsCélia Deville / Kamila Franke / Axel Mogk / Bernd Bukau / Helen R Saibil /
PubMed AbstractAAA+ 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 linksCell Rep / PubMed:31216466 / PubMed Central
MethodsEM (single particle)
Resolution3.4 - 6.2 Å
Structure data

4621

6qs4

EMDB-4621: ClpB (DWB and K476C mutant) bound to casein in presence of ATPgammaS - state KC-3
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 analogue*YM

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

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)
KeywordsCHAPERONE / disaggregase / proteostasis / AAA

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