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]]]]


<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

Crystal Structure of Chaperonin, 1pcq

E. coli GroEL/GroES complex with ADP, AlF3, Mg+2 and K+ ions (PDB entry 1pcq)

Drag the structure with the mouse to rotate

3D Structures of Chaperonin

Updated on 06-December-2015

See Heat Shock Proteins

  • 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

References