Chaperonin

(Difference between revisions)

Revision as of 14:43, 9 July 2018

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

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Updated on 09-July-2018

↑ 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
↑ 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
↑ 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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 *<scene name='44/445432/Cv/2'>E. coli GroEL/GroES complex</scene> (GroEL in green, GroES in magenta, PDB entry [[1pcq]]).
 *<scene name='44/445432/Cv/3'>GroEL/GroES complex with ADP, AlF3, Mg+2 and K+ ions</scene>.
+*<scene name='44/445432/Cv/5'>K+ ion coordination site</scene>.
+*<scene name='44/445432/Cv/6'>AlF3 binding site</scene>.
+*<scene name='44/445432/Cv/7'>Mg+2 ion coordination site</scene>.
+*<scene name='44/445432/Cv/9'>ADP binding site</scene>.
+*<scene name='44/445432/Cv/10'>Whole binding site</scene>.
 *See also [[Chaperones]].<br />
 *For GroEl in Hebrew see [[Sand box groel]].