User:Joanne Lau/sandbox 2
From Proteopedia
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===Unusual Structural Features of Hexameric ClpX=== | ===Unusual Structural Features of Hexameric ClpX=== | ||
Revision as of 05:02, 9 December 2010
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’ bacteria cells by sending specific proteins to the ‘dumpster’ and refolding others.
Intro
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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
