H
IPR027413

GroEL-like equatorial domain superfamily

InterPro entry
Short nameGROEL-like_equatorial_sf
Overlapping entries
 

Description

Chaperonins are large cylindrical structures that transiently enclose a partially folded polypeptide and allow it to continue folding in a sequestered environment. Chaperonins are grouped into two families: group I chaperonins, found in eubacteria (e.g. GroEL in Escherichia coli) and eukaryotic organelles of eubacterial descent (e.g. Cpn60 in mitochondria and chloroplasts), and group II chaperonins, found in archaea and the eukaryotic cytosol (CCT or TCP-1 complex)
[3, 1]
. Both groups share a common monomer architecture of three domains: an equatorial domain that carries ATPase activity, an intermediate domain, and an apical domain, involved in substrate binding
[2, 4, 5]
.

This superfamily represents the equatorial domain.

References

1.The chaperonin containing t-complex polypeptide 1 (TCP-1). Multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol. Kubota H, Hynes G, Willison K. Eur. J. Biochem. 230, 3-16, (1995). View articlePMID: 7601114

2.The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. Roseman AM, Chen S, White H, Braig K, Saibil HR. Cell 87, 241-51, (1996). View articlePMID: 8861908

3.Assembly of chaperonin complexes. Kusmierczyk AR, Martin J. Mol. Biotechnol. 19, 141-52, (2001). View articlePMID: 11725484

4.Crystal structure of the CCTgamma apical domain: implications for substrate binding to the eukaryotic cytosolic chaperonin. Pappenberger G, Wilsher JA, Roe SM, Counsell DJ, Willison KR, Pearl LH. J. Mol. Biol. 318, 1367-79, (2002). View articlePMID: 12083524

5.Facilitated oligomerization of mycobacterial GroEL: evidence for phosphorylation-mediated oligomerization. Kumar CM, Khare G, Srikanth CV, Tyagi AK, Sardesai AA, Mande SC. J. Bacteriol. 191, 6525-38, (2009). View articlePMID: 19717599

Cross References

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