Chaperonin

spinqualitylabelsall models E. coli GroEL (green)/GroES (magenta) 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   Print3D 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. 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. CCT or TRiC is a CPN complex found in eukarya. E. coli GroEL/GroES complex (GroEL in green, GroES in magenta, PDB entry 1pcq). GroEL/GroES complex with ADP, AlF3, Mg+2 and K+ ions. K+ ion coordination site. GroEL in cyan. AlF3 binding site. Mg+2 ion coordination site. ADP binding site. Whole binding site. See also Chaperones. For GroEl in Hebrew see Sand box groel. 3D Structures of Chaperonin Chaperonin 3D structures

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