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=''> | <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'> | ||
'''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]. | ||
Revision as of 11:30, 6 December 2015

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3D Structures of Chaperonin
Updated on 06-December-2015
- 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
- 1a6d - TaTherm α+β subunits – Thermoplasma acidophilum
References
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Jaime Prilusky, Eric Martz, Joel L. Sussman