Structural highlights
Function
THSA_THEAC Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of the substrate binding domain of the thermosome, the archaeal group II chaperonin, has been determined at 2.3 A resolution. The core resembles the apical domain of GroEL but lacks the hydrophobic residues implied in binding of substrates to group I chaperonins. Rather, a large hydrophobic surface patch is found in a novel helix-turn-helix motif, which is characteristic of all group II chaperonins including the eukaryotic TRiC/CCT complex. Models of the holochaperonin, which are consistent with cryo electron microscopy data, suggest a dual role of this helical protrusion in substrate binding and controlling access to the central cavity independent of a GroES-like cochaperonin.
Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin.,Klumpp M, Baumeister W, Essen LO Cell. 1997 Oct 17;91(2):263-70. PMID:9346243[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Klumpp M, Baumeister W, Essen LO. Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin. Cell. 1997 Oct 17;91(2):263-70. PMID:9346243
