G. Bosch et al., Crystal structure of the beta-apical domain of the thermosome reveals structural plasticity in the protrusion region, J MOL BIOL, 301(1), 2000, pp. 19-25
The crystal structure of the alpha alpha-apical domain of the thermosome, a
n archaeal group II chaperonin from Thermoplasma acidophilum, has been dete
rmined at 2.8 Angstrom resolution. The structure shows an invariant globula
r core from which a 25 Angstrom long protrusion emanates, composed of an el
ongated a-helix (H10) and a long extended stretch consisting of residues Gl
uB245-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 adopt
s an extended beta-like conformation rather than the alpha-helix seen in th
e alpha-apical domain. Consequently, it appears that the protrusions of the
apical domains from group II chaperonins might assume variety of context-d
ependent conformations during an open, substrate-accepting state of the cha
peronin. Sequence variations in the protrusion regions that are found in th
e eukaryotic TRiC/CCT subunits may provide different structural propensitie
s and hence serve different roles in substrate recognition. (C) 2000 Academ
ic Press.