Hsp104

Hsp104 is classified as a. AAA+ ATPases and a subgroup of Hsp100/Clp, because of the usage of Atp hydrolysis for structural modulation of other proteins.

Removing the aggregates without the hsp104 is insufficient there highlighting the importance of this heat shock protein and its interactions.

In hsp104 NBD1 is where ATP hydrolysis occurs, NBD2 C-terminus is shown to express the configuration of the structure by nucleotide-dependent hexamerazation.

These NBDs have diaphragms, which are conserved loops that interact in the middle of the channel inside the chaperone by coupling the ATP hydrolysis and polypeptide transport.

[5] The Hsp104 homohexamer (Figure A) is a part of an unfolding/threading mechanism that aggregates pass through and single polypeptides are extracted.

Hsp104 and Hsp70 also interact to recover native state of proteins that were exposed to heat and formed aggregates.

Some sHsps increase their molecular weight with partially folded proteins and are able to perform disaggregation by Hsp100/ClpB.

Figure A. Hsp104 Hexamer is encountering an aggregate with a chaperone it is able to extract the single polypeptides. For translocation to happen ATP hydrolysis is occurring and threading is happening to unfold proteins. Figure B. Demonstrates the crowbar model that changes shape due to conformational changes caused by the binding or hydrolysis of ATP breaking the protein aggregate. This is done in the middle of Hsp104 and later the released polypeptides can be refolded. [ 3 ]
A. Is the monomer of Hsp 104 which is composed of the N-terminal domain. Then NBD1 is shown next and is connected to the NBD2 through the linkage of small domains and middle regions which would be the Tyr residuals. Lastly, you have your C-terminal domain. B. This is the homohexamers composed of six monomers of Hsp104 and this is where they are able to deal with stressors and interact with ATP hydrolysis. [ 2 ]