The Function Of The Human Mitochondrial Chaperonin

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Crystal structure allows researchers to understand the functions of any compound. In biochemistry, structure dictates function. With the use of crystal structure analysis, scientists have a better way of analyzing specific proteins or enzymes and their function in our body. Observation of the human mitochondrial chaperonin is important because it assists in folding of mitochondrial proteins that allow for the production of energy in the cell. It also participates in specific process like apoptosis, inflammation and carcinogenesis. The study presents the structure of these human mitochondrial chaperonin to have an “American football”-shaped intermediate. It consists of two 7-membered chaperoning rings that are capped at each end. The symmetric and asymmetric bindings between the rings of the chaperonin suggest a mechanism that is distinct from the mechanism of E. Coli. Chaperonins are one our of the two types of chaperones that assist in protein folding. It does not actually participate in protein folding, but isolates aggregated protein from other compounds to be able to interact with its individual strand. It provides a stable environment that ensures proper folding. The protein comes in contact with the Gro-EL-GroES complex that has a bullet or a symmetrical football shaped complex. Here, the intermediate folding of protein is activated. They found that the human mitochondrial heat shock protein 60 (mHsp60) and its cochaperonin, human mitochondrial heat shock protein

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