Chaperonin

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. See also Chaperones.
3D Structures of Chaperonin
Updated on 15-March-2015
- 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
- 1a6d - TaTherm α+β subunits – Thermoplasma acidophilum
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