Chaperonin GroEL (GroEL)

MopA, more commonly known as Chaperonin GroEL, is a critical molecular chaperone found in most bacteria, including pathogens like Escherichia coli and Salmonella. It belongs to the Hsp60 family and works in conjunction with its co-chaperonin GroES (MopB) to facilitate the proper folding of nascent polypeptides and the refolding of denatured proteins, particularly under stress conditions such as heat shock. GroEL is essential for bacterial viability and has been implicated in antibiotic resistance, such as ceftriaxone resistance in Salmonella. Due to its fundamental role in bacterial proteostasis and virulence, GroEL is a promising target for the development of novel antimicrobial agents. Additionally, its human homolog, Hsp60, is often overexpressed in various cancers and is being explored as a target for anticancer therapies.

Other names

MopAHsp60CPN60Chaperonin 60GroL60 kDa chaperonin

Inhibition of ATPase activity, disruption of the GroEL-GroES interaction, or blocking the substrate-binding site to prevent proper protein folding.