Chaperonin

From Proteopedia

Revision as of 12:43, 13 December 2015

spinqualitylabelsall models E. coli GroEL/GroES complex with ADP, AlF3, Mg+2 and K+ ions (PDB entry 1pcq) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Crystal Structure of Chaperonin, 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.[1] The larger subunit (GroEL, CPN60) contains 3 domains: apical, intermediate and equatorial domain. The apical domain is the one which binds the polypeptide substrate. The equatorial domains binds the nucleotide. Group II CPNs are found in eukaryotic cytosol and archaea. Thermosome is a CPN complex found in archaea.[2] CCT is a CPN complex found in eukarya.[3] See also Chaperones.

3D Structures of Chaperonin

Updated on 13-December-2015

See Heat Shock Proteins

References

1. ↑ Apetri AC, Horwich AL. Chaperonin chamber accelerates protein folding through passive action of preventing aggregation. Proc Natl Acad Sci U S A. 2008 Nov 11;105(45):17351-5. doi:, 10.1073/pnas.0809794105. Epub 2008 Nov 5. PMID:18987317 doi:http://dx.doi.org/10.1073/pnas.0809794105
2. ↑ Ditzel L, Lowe J, Stock D, Stetter KO, Huber H, Huber R, Steinbacher S. Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Cell. 1998 Apr 3;93(1):125-38. PMID:9546398
3. ↑ Leitner A, Joachimiak LA, Bracher A, Monkemeyer L, Walzthoeni T, Chen B, Pechmann S, Holmes S, Cong Y, Ma B, Ludtke S, Chiu W, Hartl FU, Aebersold R, Frydman J. The Molecular Architecture of the Eukaryotic Chaperonin TRiC/CCT. Structure. 2012 May 9;20(5):814-25. Epub 2012 Apr 12. PMID:22503819 doi:10.1016/j.str.2012.03.007