Molecular Playground/E. coli ClpP

From Proteopedia

Revision as of 16:22, 3 December 2014

Here in the Chien lab, we study how degradation plays a large part in protein quality control. The maintenance and timely destruction of protein levels plays an important role during cell homeostasis and cell transitions/differentiation, yet much of what governs these processes has yet to be fully understood.

Introduction

{i}E. coli{i} Casein lytic proteinase P (ClpP) is a double ring tetradecameric homo oligomer compartmentalized peptidase [1]. ClpP requires the use of ATP dependent regulatory elements that independently bind to ClpP in order for substrates to have access the active core [2-4]. Here, proteins that are translocated by regulatory elements into the peptidase core are cleaved into smaller amino acid chains approximately on average 6-8aa in length [5].

spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Proteolysis and ClpP Contents 1 Function 2 Our research interest 3 Relevance 4 Structural highlights Function Our research interest Relevance Structural highlights This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

References

Acknowledgements

Kamal Joshi, Joanne Lau, Jing Liu, Rob Vass