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Chaperonin

From Proteopedia

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Line 20: Line 20:
**[[3m6c]] – MtGroEL1 apical domain – ''Mycobacterium tuberculosis''<BR />
**[[3m6c]] – MtGroEL1 apical domain – ''Mycobacterium tuberculosis''<BR />
**[[1sjp]], [[3rtk]] – MtGroEL2 residues 42-539<BR />
**[[1sjp]], [[3rtk]] – MtGroEL2 residues 42-539<BR />
-
**[[2eu1]], [[4v43]], [[1oel]], [[1grl]], [[2yey]] – EcGroEL (mutant) - ''Escherichia coli''<BR />
+
**[[2eu1]], [[4v43]], [[1oel]], [[1grl]], [[2yey]], [[4wsc]], [[4wgl]] – EcGroEL (mutant) - ''Escherichia coli''<BR />
**[[3e76]], [[2nwc]], [[1xck]], [[1ss8]], [[4hel]] – EcGroEL<BR />
**[[3e76]], [[2nwc]], [[1xck]], [[1ss8]], [[4hel]] – EcGroEL<BR />
**[[3c9v]], [[3cau]], [[2ynj]] – EcGroEL – Cryo EM<BR />
**[[3c9v]], [[3cau]], [[2ynj]] – EcGroEL – Cryo EM<BR />
Line 41: Line 41:
**[[1mnf]] – EcGroEL + polypeptide<BR />
**[[1mnf]] – EcGroEL + polypeptide<BR />
**[[2cgt]] – EcGroEL + capsid assbly protein GP31 – EM<BR />
**[[2cgt]] – EcGroEL + capsid assbly protein GP31 – EM<BR />
-
**[[1dkd]] - EcGroEL apical domain + polypeptide
+
**[[1dkd]] - EcGroEL apical domain + polypeptide<br />
 +
**[[4pj1]] - GroEL + ADP – human<br />
*''Small subunit''
*''Small subunit''
Line 100: Line 101:
**[[1q3q]] - TkTherm α subunit (mutant) + AMP-PNP<br />
**[[1q3q]] - TkTherm α subunit (mutant) + AMP-PNP<br />
**[[1q3s]] - TkTherm α subunit (mutant) + ADP<br />
**[[1q3s]] - TkTherm α subunit (mutant) + ADP<br />
 +
**[[4xcd]] - SsTherm β subunit + ADP – ''Sulfolobus solfataricus''<br />
 +
**[[4xcg]], [[4xci]] - SsTherm α+β subunits + ADP<br />
**[[1lep]] – CPN-10 – ''Mycobacterium leprae''
**[[1lep]] – CPN-10 – ''Mycobacterium leprae''

Revision as of 08:21, 2 April 2017

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 02-April-2017

See Heat Shock Proteins

References

  1. ↑ 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
  2. ↑ Ditzel L, Lowe J, Stock D, Stetter KO, Huber H, Huber R, Steinbacher S. Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Cell. 1998 Apr 3;93(1):125-38. PMID:9546398
  3. ↑ Leitner A, Joachimiak LA, Bracher A, Monkemeyer L, Walzthoeni T, Chen B, Pechmann S, Holmes S, Cong Y, Ma B, Ludtke S, Chiu W, Hartl FU, Aebersold R, Frydman J. The Molecular Architecture of the Eukaryotic Chaperonin TRiC/CCT. Structure. 2012 May 9;20(5):814-25. Epub 2012 Apr 12. PMID:22503819 doi:10.1016/j.str.2012.03.007
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