Chaperonin: Difference between revisions
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[[Image:1pcq.png|left|200px|thumb|Crystal Structure of Chaperonin, [[1pcq]]]] | [[Image:1pcq.png|left|200px|thumb|Crystal Structure of Chaperonin, [[1pcq]]]] | ||
{{STRUCTURE_1pcq| PDB=1pcq | SIZE=300| SCENE= |right|CAPTION=GroEL/GroES complex, [[1pcq]] }} | {{STRUCTURE_1pcq| PDB=1pcq | SIZE=300| SCENE=Chaperonin/Groel_groes_comnplex/1 |right|CAPTION=GroEL/GroES complex, [[1pcq]] }} | ||
Chaperonin (CPN) are oligomeric proteins which mediate the folding of polypeptide chains. Group I CPNs are found in bacteria, chloroplasts and mitochondria. They include the most characterized 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. | Chaperonin (CPN) are oligomeric proteins which mediate the folding of polypeptide chains. Group I CPNs are found in bacteria, chloroplasts and mitochondria. They include the most characterized 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. | ||
