User:Joanne Lau/sandbox 2

From Proteopedia

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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 protein ‘spring cleans’ the cell by sending specific proteins to the ‘dumpster’.

Intro

Contents 1 Unusual Features of the Hexameric ClpX 2 ClpX as an ATPase 3 Central Pore of the Hexameric ClpX is Conserved 4 How ClpX recognizes specific proteins 5 Interaction between ClpX and peptidase ClpP gives rise to Protein Degradation Machinery

Unusual Features of the Hexameric ClpX

Asymmetry and Falls into two classes of subunits

ClpX as an ATPase

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

Central Pore of the Hexameric ClpX is Conserved

Central pore is critical, conserved.

How ClpX recognizes specific proteins

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

Interaction between ClpX and peptidase ClpP gives rise to 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.

References