Chaperonins

14- 7 in each layer

12- 6 in each layer

10- 5 in each layer

Creates a space away from crowded cytosol for protein binding

Creates a highly acidic environment for proteins to fold in

Allows protein to fold in highly saline environment

At the same

Opposite

10-15

15-20

20-25

A nascent polypeptide binds to the end opposite the Gro-Es and ADP, causing the cycle to repeat itself at the other end of the protein

Gro-Es dissociates, releasing the folded protein

The ADP is released and replaced with ATP

Clp

Clr

Cld

Class 1- Protein degredation
Class 2- Protein disaggregation and refolding

Class 1- Protein disaggregation and refolding
Class 2- Protein degredation

Class 1 has 2 ATPase sites, Class 2 has 1

Class 1 has 1 ATPase site, Class 2 has 2

To drive conformational changes in aromatic loops that interact with the substrate

To provide energy to break the peptide bonds in the protein to be unfolded

To provide energy to posh apart poorly stacked peptides

High temperature growth

High salinity growth

High pH growth

ATP binding site

Substrate binding domain

Dimerisation domain

N terminus

C terminus

Middle

Binding it to Hsp70

Preventing N-terminal dimerisation

Phosphorylation of Hsp90

Activates ATPase activity by promoting open state of of catalytic loop

Causing N-terminal alignment for dimerisation

Physically holding the active site open

Interacts with the middle domain of Hsp90 and modulates the catalytic loop of this domain

Increases the affinity of the dimerisation sites for each other, completing the ATPase sites more stably

Increases the affinity for the binding site for ATP