1ass
|
APICAL DOMAIN OF THE CHAPERONIN FROM THERMOPLASMA ACIDOPHILUM
OverviewOverview
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.
About this StructureAbout this Structure
1ASS is a Single protein structure of sequence from Thermoplasma acidophilum with NA and PO4 as ligands. Full crystallographic information is available from OCA.
ReferenceReference
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
Page seeded by OCA on Tue Nov 20 11:06:39 2007