1asx

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spinqualitylabelsall models 1asx, resolution 2.8Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

APICAL DOMAIN OF THE CHAPERONIN FROM THERMOPLASMA ACIDOPHILUM

Overview

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 Structure

1ASX is a Single protein structure of sequence from Thermoplasma acidophilum with PO4 as ligand. Full crystallographic information is available from OCA.

Reference

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

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