Crystal structure of the β-Apical domain of the thermosome reveals structural plasticity in the protrusion region

Gundula Bosch, Wolfgang Baumeister, Lars Oliver Essen

Research output: Contribution to journalArticle

Abstract

The crystal structure of the β-apical domain of the thermosome, an archaeal group II chaperonin from Thermoplasma acidophilum, has been determined at 2.8 Å resolution. The structure shows an invariant globular core from which a 25 Å long protrusion emanates, composed of an elongated α-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 β-like conformation rather than the α-helix seen in the α-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. (C) 2000 Academic Press.

Original languageEnglish (US)
Pages (from-to)19-25
Number of pages7
JournalJournal of Molecular Biology
Volume301
Issue number1
DOIs
StatePublished - Aug 4 2000
Externally publishedYes

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Thermosomes
Group II Chaperonins
Thermoplasma
Chaperonins

Keywords

  • Apical domain
  • Chaperonin
  • Crystal structure
  • Thermoplasma acidophilum
  • Thermosome

ASJC Scopus subject areas

  • Virology

Cite this

Crystal structure of the β-Apical domain of the thermosome reveals structural plasticity in the protrusion region. / Bosch, Gundula; Baumeister, Wolfgang; Essen, Lars Oliver.

In: Journal of Molecular Biology, Vol. 301, No. 1, 04.08.2000, p. 19-25.

Research output: Contribution to journalArticle

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abstract = "The crystal structure of the β-apical domain of the thermosome, an archaeal group II chaperonin from Thermoplasma acidophilum, has been determined at 2.8 {\AA} resolution. The structure shows an invariant globular core from which a 25 {\AA} long protrusion emanates, composed of an elongated α-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 β-like conformation rather than the α-helix seen in the α-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. (C) 2000 Academic Press.",
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AU - Essen, Lars Oliver

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N2 - The crystal structure of the β-apical domain of the thermosome, an archaeal group II chaperonin from Thermoplasma acidophilum, has been determined at 2.8 Å resolution. The structure shows an invariant globular core from which a 25 Å long protrusion emanates, composed of an elongated α-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 β-like conformation rather than the α-helix seen in the α-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. (C) 2000 Academic Press.

AB - The crystal structure of the β-apical domain of the thermosome, an archaeal group II chaperonin from Thermoplasma acidophilum, has been determined at 2.8 Å resolution. The structure shows an invariant globular core from which a 25 Å long protrusion emanates, composed of an elongated α-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 β-like conformation rather than the α-helix seen in the α-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. (C) 2000 Academic Press.

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