User:Joanne Lau/sandbox 2

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One of the CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground.

Molecular Playground banner: "ClpX ‘spring cleans’ by dumping some proteins and refolding others. More at MolecularPlayground.org."

Intro

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Drag the structure with the mouse to rotate

Contents

Unusual Structural Features of Hexameric ClpX

Central Pore of the Hexameric ClpX is Conserved, Asymmetry, Falls into two classes of subunits


How ClpX Recognizes Specific Proteins

Itself can recognize proteins with certain motifs. Adaptors enhance reactivity, sspB, Rssb.

Hexameric ClpX Unfolds and Drives Proteins Through its Aperture

Angle changes and height changes, pulling a protein through to unfold it

Interaction between ClpX and ClpP results in a powerful Protein Degradation Machinery

Interaction between ClpX and ClpP donut in a row, which domain interacts. Critical to determine ClpX role as a chaperone or a protease. How powerful

References

Proteopedia Page Contributors and Editors (what is this?)

Joanne Lau

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