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  Crystal structure of the beta-apical domain of the thermosome reveals structural plasticity in the protrusion region

Bosch, G., Baumeister, W., & Essen, L. O. (2000). Crystal structure of the beta-apical domain of the thermosome reveals structural plasticity in the protrusion region. Journal of Molecular Biology, 301(1), 19-25.

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Genre: Zeitschriftenartikel
Alternativer Titel : J. Mol. Biol

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Bosch, G.1, Autor           
Baumeister, W.1, Autor           
Essen, L. O., Autor
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1External Organizations, ou_persistent22              

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Schlagwörter: Chaperonin; Thermosome; Thermoplasma acidophilum; Apical domain; Crystal structure.; Group-ii chaperonins; Archaeal chaperonin; Folding machine; Binding domains; Ef-tu; Protein; Groel; Cct; Conformation; Subunits.; Molecular Biology & Genetics in Current Contents(R)/Life Sciences.
 Zusammenfassung: The crystal structure of the alpha alpha-apical domain of the thermosome, an archaeal group II chaperonin from Thermoplasma acidophilum, has been determined at 2.8 Angstrom resolution. The structure shows an invariant globular core from which a 25 Angstrom long protrusion emanates, composed of an elongated a-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 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. [References: 40]

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 Datum: 2000
 Publikationsstatus: Erschienen
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Titel: Journal of Molecular Biology
  Alternativer Titel : J. Mol. Biol
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 301 (1) Artikelnummer: - Start- / Endseite: 19 - 25 Identifikator: -