1E0R

Beta-apical domain of thermosome

Summary for 1E0R

• Entry DOI: 10.2210/pdb1e0r/pdb
• Related: 1A6D 1A6E 1ASS 1ASX
• Descriptor: THERMOSOME (1 entity in total)
• Functional Keywords: chaperonin, hsp60, thermosome, tcp1, groel, thermoplasma acidophilum
• Biological source: THERMOPLASMA ACIDOPHILUM
• Total number of polymer chains: 1
• Total formula weight: 17763.39

Authors

Bosch, G.,Baumeister, W.,Essen, L.-O. (deposition date: 2000-04-06, release date: 2000-08-19, Last modification date: 2023-12-06)

Primary citation

Bosch, G.,Baumeister, W.,Essen, L.-O.
Crystal Structure of the Beta-Apical Domain from Thermosome Reveals Structural Plasticity in Protrusion Region
J.Mol.Biol., 301:19-, 2000

PubMed Abstract: The crystal structure of the beta-apical domain of the thermosome, an archaeal group II chaperonin from Thermoplasma acidophilum, has been determined at 2.8 A resolution. The structure shows an invariant globular core from which a 25 A long protrusion emanates, composed of an elongated alpha-helix (H10) and a long extended stretch consisting of residues GluB245-ThrB253. A comparison with previous apical domain structures reveals a large segmental displacement of the protruding part of helix H10 via the hinge GluB276-ValB278. The region comprising residues GluB245-ThrB253 adopts an extended beta-like conformation rather than the alpha-helix seen in the alpha-apical domain. Consequently, it appears that the protrusions of the apical domains from group II chaperonins might assume a variety of context-dependent conformations during an open, substrate-accepting state of the chaperonin. Sequence variations in the protrusion regions that are found in the eukaryotic TRiC/CCT subunits may provide different structural propensities and hence serve different roles in substrate recognition.

PubMed: 10926489
DOI: 10.1006/JMBI.2000.3955

Experimental method

X-RAY DIFFRACTION (2.8 Å)