Abstract by Sean Zocca

Personal Infomation

Presenter's Name

Sean Zocca

Degree Level



Jorge Cuéllar
Takuma Aoba
W.Grant Ludlam
Madhura Dhavale
Nicole C Tensmeyer
Rebecca L Plimpton
Aman Makaju
Sarah Franklin
Barry M Willardson

Abstract Infomation


Chemistry and Biochemistry

Faculty Advisor

Barry Willardson


Structure of the mLST8-CCT Folding Complex


mLST8 is a key component found in mTORC1 and mTORC2 protein complexes.  The mTORC complexes are key regulators of cell growth, metabolism and control important cellular processes such as protein synthesis, energy metabolism and so forth. As a result, mTORC components represent high-value therapeutic drug targets. Studies have been conducted on how mTOR complexes regulate protein synthesis but there is not much that is known about how the subunits of mTOR are assembled from their nascent polypeptides.  We show that the cytosolic chaperonin containing TCP-1(CCT) is the chaperone responsible for folding mLST8. We have been able to isolate mLST8 bound to CCT in a folding intermediate. Through single particle cryo electron microscopy we were able to obtain a reconstruction of the intermediate at a resolution of 3.98 angstrom. This structure represents the highest resolution of a folding substrate inside the CCT cavity to date