InterPro : IPR027413

Name  GroEL-like equatorial domain Short Name  GROEL-like_equatorial
Type  Domain 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 organellesof 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) [, ]. 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 substratebinding [, , ].This entry represents the equatorial domain.
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Proteins

InterPro protein domain ID --> Contigs

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5 Publications

First Author Title Year Journal Volume Pages
Pappenberger G Crystal structure of the CCTgamma apical domain: implications for substrate binding to the eukaryotic cytosolic chaperonin. 2002 J Mol Biol 318 1367-79
Kusmierczyk AR Assembly of chaperonin complexes. 2001 Mol Biotechnol 19 141-52
Roseman AM The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. 1996 Cell 87 241-51
Kubota H The chaperonin containing t-complex polypeptide 1 (TCP-1). Multisubunit machinery assisting in protein folding and assembly in the eukaryotic cytosol. 1995 Eur J Biochem 230 3-16
Kumar CM Facilitated oligomerization of mycobacterial GroEL: evidence for phosphorylation-mediated oligomerization. 2009 J Bacteriol 191 6525-38



To cite PlanMine, please refer to the following publication:

Brandl, H., Moon, H., Vila-Farré, M., Liu, S.-Y., Henry, I., & Rink, J. C.
PlanMine - a mineable resource of planarian biology and biodiversity.
Nucleic Acids Research, gkv1148. doi:10.1093/nar/gkv1148 (2015)