PS00681

Chaperonins cpn10 signature

PROSITE patterns entry
Member databasePROSITE patterns
PROSITE patterns typeconserved site
Short nameCHAPERONINS_CPN10

Description

Chaperonins
[4]
are proteins involved in the folding of proteins or the assembly of oligomeric protein complexes. They seem to assist other polypeptides in maintaining or assuming conformations which permit their correct assembly into oligomeric structures. They are found in abundance in prokaryotes, chloroplasts and mitochondria. Chaperonins form oligomeric complexes and are composed of two different types of subunits: a 60 Kd protein, known as cpn60 (groEL in bacteria) and a 10 Kd protein, known as cpn10 (groES in bacteria). The cpn10 protein binds to cpn60 in the presence of MgATP and suppresses the ATPase activity of the latter. Cpn10 is a protein of about 100 amino acid residues whose sequence is well conserved in bacteria, vertebrate mitochondria and plants chloroplast
[2]
[1]
. Cpn10 assembles as an heptamer that forms a dome
[3]
. As a signature pattern for cpn10 we selected a region located in the N- terminal section of the protein.

References

1.Identification, characterization, and DNA sequence of a functional "double" groES-like chaperonin from chloroplasts of higher plants. Bertsch U, Soll J, Seetharam R, Viitanen PV. Proc. Natl. Acad. Sci. U.S.A. 89, 8696-700, (1992). View articlePMID: 1356267

2.Identification of a mammalian 10-kDa heat shock protein, a mitochondrial chaperonin 10 homologue essential for assisted folding of trimeric ornithine transcarbamoylase in vitro. Hartman DJ, Hoogenraad NJ, Condron R, Hoj PB. Proc. Natl. Acad. Sci. U.S.A. 89, 3394-8, (1992). View articlePMID: 1348860

3.The crystal structure of the GroES co-chaperonin at 2.8 A resolution. Hunt JF, Weaver AJ, Landry SJ, Gierasch L, Deisenhofer J. Nature 379, 37-45, (1996). View articlePMID: 8538739

4.Molecular chaperones. Ellis RJ, van der Vies SM. Annu. Rev. Biochem. 60, 321-47, (1991). View articlePMID: 1679318

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