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1asx
From Proteopedia
| 1asx, resolution 2.80Å () | |||||||||
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| Ligands: | |||||||||
| Gene: | THSA (Thermoplasma acidophilum) | ||||||||
| Related: | 1ass | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
APICAL DOMAIN OF THE CHAPERONIN FROM THERMOPLASMA ACIDOPHILUM
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1asx is a 1 chain structure with sequence from Thermoplasma acidophilum. Full crystallographic information is available from OCA.
See Also
Reference
- 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
Categories: Thermoplasma acidophilum | Baumeister, W. | Essen, L O. | Klumpp, M. | Atp-binding | Chaperonin | Groel | Hsp60 | Tcp1 | Thermosome
