1ASX
APICAL DOMAIN OF THE CHAPERONIN FROM THERMOPLASMA ACIDOPHILUM
Summary for 1ASX
| Entry DOI | 10.2210/pdb1asx/pdb |
| Related | 1ASS |
| Descriptor | THERMOSOME, PHOSPHATE ION (3 entities in total) |
| Functional Keywords | chaperonin, hsp60, thermosome, tcp1, groel, thermoplasma acidophilum, atp-binding |
| Biological source | Thermoplasma acidophilum |
| Total number of polymer chains | 1 |
| Total formula weight | 17917.60 |
| Authors | Klumpp, M.,Baumeister, W.,Essen, L.-O. (deposition date: 1997-08-11, release date: 1997-12-03, Last modification date: 2024-05-22) |
| Primary citation | Klumpp, M.,Baumeister, W.,Essen, L.O. Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin. Cell(Cambridge,Mass.), 91:263-270, 1997 Cited by PubMed Abstract: 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. PubMed: 9346243DOI: 10.1016/S0092-8674(00)80408-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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