What is it about?

We have visualised a binary complex of the denatured substrate protein (also called as non-native protein) bound to the classic chaperonin GroEL. It is usually expected that a non-native protein may not have any folded domain feature. But, to our surprise, a distinct domain like features were observed in the bound non-native protein. This was possible by single-particle cryoEM and three dimensional image processing of heterogenous particles into three distinct classes using available cryoEM image processing algorithms.

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Why is it important?

RuBisCO bound to GroEL as binary complex were extensively used to characterise the Chaperonin GroEL in 1970's. But the structural visualisation of binary complex was a challenging one. We have visualised this binary complex for the first time. This provides some interesting results.

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This page is a summary of: A two-domain folding intermediate of RuBisCO in complex with the GroEL chaperonin, International Journal of Biological Macromolecules, October 2018, Elsevier,
DOI: 10.1016/j.ijbiomac.2018.06.120.
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