Chaperonin

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Revision as of 09:33, 20 November 2014 by Michal Harel (talk | contribs)
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Crystal Structure of Chaperonin, 1pcq

Template:STRUCTURE 1pcq













Chaperonins (CPN) are oligomeric proteins that mediate the folding of polypeptide chains. Group I CPN are found in bacteria, chloroplasts and mitochondria. For an introductory overview, see Chaperonins in Wikipedia.

The most characterized CPN are in the GroEL/GroES complex from Escherichia coli and CPN60/CPN10 from Thermus thermophilus. The larger subunit (GroEL, CPN60) contains 3 domains. The apical domain is the one which binds the substrate. Group II CPNs are found in eukaryotic cytosol and archaea. Thermosome is a CPN complex found in archaea. CCT is a CPN complex found in eukarya.

3D Structures of Chaperonin

Updated on 20-November-2014

See Heat Shock Proteins

  • Thermosome
    • 1a6d - TaTherm α+β subunits – Thermoplasma acidophilum
    • 1a6e - TaTherm α+β subunits + ADP
    • 1ass, 1asx - TaTherm α apical domain
    • 1e0r – TaTherm β apical domain
    • 3ko1 – AtTherm α subunit– Acidianus tengchongensis
    • 3j1b, 3j1c, 3j1e - AtTherm α subunit – Cryo EM
    • 3j1f - AtTherm β subunit + ATP – Cryo EM
    • 3aq1 – Therm – Methanococcoides burtonii
    • 1q2v, 1q3r – TkTherm α subunit (mutant) – Thermococcus KS-1
    • 1q3q - TkTherm α subunit (mutant) + AMP-PNP
    • 1q3s - TkTherm α subunit (mutant) + ADP
    • 1lep – CPN-10 – Mycobacterium leprae