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| Verfasst von: | Chiapparino, Antonella [VerfasserIn]  |
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| | Grbavac, Antonija [VerfasserIn] |
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| | Jonker, Hendrik RA [VerfasserIn] |
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| | Hackmann, Yvonne [VerfasserIn] |
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| | Mortensen, Sofia [VerfasserIn] |
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| | Zatorska, Ewa [VerfasserIn] |
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| | Schott, Andrea [VerfasserIn] |
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| | Stier, Gunter [VerfasserIn] |
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| | Saxena, Krishna [VerfasserIn] |
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| | Wild, Klemens [VerfasserIn] |
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| | Schwalbe, Harald [VerfasserIn] |
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| | Strahl, Sabine [VerfasserIn] |
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| | Sinning, Irmgard [VerfasserIn] |
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| Titel: | Functional implications of MIR domains in protein O-mannosylation |
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| Verf.angabe: | Antonella Chiapparino, Antonija Grbavac, Hendrik RA Jonker, Yvonne Hackmann, Sofia Mortensen, Ewa Zatorska, Andrea Schott, Gunter Stier, Krishna Saxena, Klemens Wild, Harald Schwalbe, Sabine Strahl, Irmgard Sinning |
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| E-Jahr: | 2020 |
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| Jahr: | 24 December 2020 |
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| Umfang: | 23 S. |
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| Fussnoten: | Gesehen am 17.02.2022 |
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| Titel Quelle: | Enthalten in: eLife |
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| Ort Quelle: | Cambridge : eLife Sciences Publications, 2012 |
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| Jahr Quelle: | 2020 |
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| Band/Heft Quelle: | 9(2020), Artikel-ID e61189, Seite 1-23 |
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| ISSN Quelle: | 2050-084X |
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| Abstract: | Protein O-mannosyltransferases (PMTs) represent a conserved family of multispanning endoplasmic reticulum membrane proteins involved in glycosylation of S/T-rich protein substrates and unfolded proteins. PMTs work as dimers and contain a luminal MIR domain with a β-trefoil fold, which is susceptive for missense mutations causing α-dystroglycanopathies in humans. Here, we analyze PMT-MIR domains by an integrated structural biology approach using X-ray crystallography and NMR spectroscopy and evaluate their role in PMT function in vivo. We determine Pmt2- and Pmt3-MIR domain structures and identify two conserved mannose-binding sites, which are consistent with general β-trefoil carbohydrate-binding sites (α, β), and also a unique PMT2-subfamily exposed FKR motif. We show that conserved residues in site α influence enzyme processivity of the Pmt1-Pmt2 heterodimer in vivo. Integration of the data into the context of a Pmt1-Pmt2 structure and comparison with homologous β-trefoil - carbohydrate complexes allows for a functional description of MIR domains in protein O-mannosylation. |
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| DOI: | doi:10.7554/eLife.61189 |
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| URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext: https://doi.org/10.7554/eLife.61189 |
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| | DOI: https://doi.org/10.7554/eLife.61189 |
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| Datenträger: | Online-Ressource |
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| Sprache: | eng |
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| Sach-SW: | carbohydrate-binding module |
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| | enzymatic processivity |
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| | glycosyltransferase |
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| | NMR |
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| | protein O-mannosylation |
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| | x-ray crystallography |
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| K10plus-PPN: | 1789500575 |
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| Verknüpfungen: | → Zeitschrift |
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Functional implications of MIR domains in protein O-mannosylation / Chiapparino, Antonella [VerfasserIn]; 24 December 2020 (Online-Ressource)
