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Structure paper

TitleStructural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase.
Journal, issue, pagesNat Commun, Vol. 10, Issue 1, Page 2393, Year 2019
Publish dateJun 3, 2019
AuthorsAlexandrea N Rizo / JiaBei Lin / Stephanie N Gates / Eric Tse / Stephen M Bart / Laura M Castellano / Frank DiMaio / James Shorter / Daniel R Southworth /
PubMed AbstractBacterial ClpB and yeast Hsp104 are homologous Hsp100 protein disaggregases that serve critical functions in proteostasis by solubilizing protein aggregates. Two AAA+ nucleotide binding domains (NBDs) ...Bacterial ClpB and yeast Hsp104 are homologous Hsp100 protein disaggregases that serve critical functions in proteostasis by solubilizing protein aggregates. Two AAA+ nucleotide binding domains (NBDs) power polypeptide translocation through a central channel comprised of a hexameric spiral of protomers that contact substrate via conserved pore-loop interactions. Here we report cryo-EM structures of a hyperactive ClpB variant bound to the model substrate, casein in the presence of slowly hydrolysable ATPγS, which reveal the translocation mechanism. Distinct substrate-gripping interactions are identified for NBD1 and NBD2 pore loops. A trimer of N-terminal domains define a channel entrance that binds the polypeptide substrate adjacent to the topmost NBD1 contact. NBD conformations at the seam interface reveal how ATP hydrolysis-driven substrate disengagement and re-binding are precisely tuned to drive a directional, stepwise translocation cycle.
External linksNat Commun / PubMed:31160557 / PubMed Central
MethodsEM (single particle)
Resolution2.9 - 4.1 Å
Structure data

20004

6oax

EMDB-20004: CryoEM map of the hyperactive ClpB mutant K476C, bound to casein, pre-state
PDB-6oax: Structure of the hyperactive ClpB mutant K476C, bound to casein, pre-state
Method: EM (single particle) / Resolution: 2.9 Å

20005

6oay

EMDB-20005: CryoEM map of the hyperactive ClpB mutant K476C, bound to casein, post-state
PDB-6oay: Structure of the hyperactive ClpB mutant K476C, bound to casein, post-state
Method: EM (single particle) / Resolution: 3.3 Å

20049

6og1

EMDB-20049: CryoEM focus classification map of the hyperactive ClpB mutant K476C, bound to casein, pre-state
PDB-6og1: Focus classification structure of the hyperactive ClpB mutant K476C, bound to casein, pre-state
Method: EM (single particle) / Resolution: 3.3 Å

20050

6og2

EMDB-20050: CryoEM focus classification map of the hyperactive ClpB mutant K476C, bound to casein, post-state
PDB-6og2: Focus classification structure of the hyperactive ClpB mutant K476C, bound to casein, post-state
Method: EM (single particle) / Resolution: 4.1 Å

20051

6og3

EMDB-20051: CryoEM focus classification map of the hyperactive ClpB mutant K476C, bound to casein, NTD-trimer
PDB-6og3: Focus classification structure of the hyperactive ClpB mutant K476C, bound to casein, NTD-trimer
Method: EM (single particle) / Resolution: 4.1 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 / Adenosine diphosphate

Source
  • escherichia coli k-12 (bacteria)
  • bos taurus (cattle)
KeywordsCHAPERONE / disaggregase / CLPB / AAA+

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