Chaperonin
From Proteopedia
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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]]]] | ||
| - | <StructureSection load='1pcq' size='350' side='right' caption='GroEL/GroES complex with ADP, AlF3, Mg+2 and K+ ions (PDB entry [[1pcq]])' scene='Chaperonin/Groel_groes_comnplex/1'> | + | <StructureSection load='1pcq' size='350' side='right' caption='E. coli GroEL/GroES complex with ADP, AlF3, Mg+2 and K+ ions (PDB entry [[1pcq]])' scene='Chaperonin/Groel_groes_comnplex/1'> |
| - | '''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 [http://en.wikipedia.org/wiki/Chaperonins Chaperonins in Wikipedia]. | + | '''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 [http://en.wikipedia.org/wiki/Chaperonins 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. | + | The most characterized CPN are in the GroEL/GroES complex from ''Escherichia coli'' and CPN60/CPN10 from ''Thermus thermophilus''.<ref>PMID:18987317</ref> 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]]. | See also [[Chaperones]]. | ||
</StructureSection> | </StructureSection> | ||
Revision as of 11:36, 6 December 2015
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3D Structures of Chaperonin
Updated on 06-December-2015
References
- ↑ 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
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