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doi:10.22028/D291-44436
Titel: | Structural features of chloroplast trigger factor determined at 2.6 Å resolution |
VerfasserIn: | Carius, Yvonne Fries, Fabian Norbert Gries, Karin Trentmann, Oliver Lancaster, C Roy D Willmund, Felix |
Sprache: | Englisch |
Titel: | Acta crystallographica |
Bandnummer: | 78 |
Heft: | Pt 10 |
Seiten: | 1259-1272 |
Verlag/Plattform: | Wiley |
Erscheinungsjahr: | 2022 |
Freie Schlagwörter: | molecular chaperones chaperone trigger factor chloroplasts Chlamydomonas reinhardtii co-translational folding PPIases |
DDC-Sachgruppe: | 610 Medizin, Gesundheit |
Dokumenttyp: | Journalartikel / Zeitschriftenartikel |
Abstract: | The folding of newly synthesized polypeptides requires the coordinated action of molecular chaperones. Prokaryotic cells and the chloroplasts of plant cells possess the ribosome-associated chaperone trigger factor, which binds nascent polypeptides at their exit stage from the ribosomal tunnel. The structure of bacterial trigger factor has been well characterized and it has a dragon-shaped conformation, with flexible domains responsible for ribosome binding, peptidyl-prolyl cis-trans isomerization (PPIase) activity and substrate protein binding. Chloroplast trigger-factor sequences have diversified from those of their bacterial orthologs and their molecular mechanism in plant organelles has been little investigated to date. Here, the crystal structure of the plastidic trigger factor from the green alga Chlamydomonas reinhardtii is presented at 2.6 Å resolution. Due to the high intramolecular flexibility of the protein, diffraction to this resolution was only achieved using a protein that lacked the N-terminal ribosome-binding domain. The eukaryotic trigger factor from C. reinhardtii exhibits a comparable dragon-shaped conformation to its bacterial counterpart. However, the C-terminal chaperone domain displays distinct charge distributions, with altered positioning of the helical arms and a specifically altered charge distribution along the surface responsible for substrate binding. While the PPIase domain shows a highly conserved structure compared with other PPIases, its rather weak activity and an unusual orientation towards the C-terminal domain points to specific adaptations of eukaryotic trigger factor for function in chloroplasts. |
DOI der Erstveröffentlichung: | 10.1107/S2059798322009068 |
URL der Erstveröffentlichung: | https://journals.iucr.org/d/issues/2022/10/00/jv5013/index.html |
Link zu diesem Datensatz: | urn:nbn:de:bsz:291--ds-444363 hdl:20.500.11880/39698 http://dx.doi.org/10.22028/D291-44436 |
ISSN: | 2059-7983 0907-4449 |
Datum des Eintrags: | 19-Feb-2025 |
Fakultät: | M - Medizinische Fakultät |
Fachrichtung: | M - Augenheilkunde M - Biophysik |
Professur: | M - Prof. Dr. C. Roy D. Lancaster M - Prof. Dr. med. Nóra Szentmáry |
Sammlung: | SciDok - Der Wissenschaftsserver der Universität des Saarlandes |
Dateien zu diesem Datensatz:
Datei | Beschreibung | Größe | Format | |
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jv5013.pdf | 2,01 MB | Adobe PDF | Öffnen/Anzeigen |
Diese Ressource wurde unter folgender Copyright-Bestimmung veröffentlicht: Lizenz von Creative Commons