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Functional implications of MIR domains in protein O-mannosylation.
Chiapparino, Antonella; Grbavac, Antonija; Jonker, Hendrik Ra; Hackmann, Yvonne; Mortensen, Sofia; Zatorska, Ewa; Schott, Andrea; Stier, Gunter; Saxena, Krishna; Wild, Klemens; Schwalbe, Harald; Strahl, Sabine; Sinning, Irmgard.
Afiliación
  • Chiapparino A; Heidelberg University Biochemistry Center (BZH), Heidelberg, Germany.
  • Grbavac A; Centre for Organismal Studies (COS), Heidelberg University, Heidelberg, Germany.
  • Jonker HR; Institute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Goethe University, Frankfurt am Main, Germany.
  • Hackmann Y; Heidelberg University Biochemistry Center (BZH), Heidelberg, Germany.
  • Mortensen S; Heidelberg University Biochemistry Center (BZH), Heidelberg, Germany.
  • Zatorska E; Centre for Organismal Studies (COS), Heidelberg University, Heidelberg, Germany.
  • Schott A; Centre for Organismal Studies (COS), Heidelberg University, Heidelberg, Germany.
  • Stier G; Heidelberg University Biochemistry Center (BZH), Heidelberg, Germany.
  • Saxena K; Institute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Goethe University, Frankfurt am Main, Germany.
  • Wild K; Heidelberg University Biochemistry Center (BZH), Heidelberg, Germany.
  • Schwalbe H; Institute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Goethe University, Frankfurt am Main, Germany.
  • Strahl S; Centre for Organismal Studies (COS), Heidelberg University, Heidelberg, Germany.
  • Sinning I; Heidelberg University Biochemistry Center (BZH), Heidelberg, Germany.
Elife ; 92020 12 24.
Article en En | MEDLINE | ID: mdl-33357379
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 ß-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 ß-trefoil carbohydrate-binding sites (α, ß), 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 ß-trefoil - carbohydrate complexes allows for a functional description of MIR domains in protein O-mannosylation.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Conformación Proteica / Manosiltransferasas Límite: Animals / Humans Idioma: En Revista: Elife Año: 2020 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido
Texto completo
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Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Conformación Proteica / Manosiltransferasas Límite: Animals / Humans Idioma: En Revista: Elife Año: 2020 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido