6ZQQ
Structure of the Pmt3-MIR domain with bound ligands
Summary for 6ZQQ
| Entry DOI | 10.2210/pdb6zqq/pdb |
| Descriptor | PMT3 isoform 1, GLYCEROL (3 entities in total) |
| Functional Keywords | carbohydrate-binding module, mir domain, protein-o-mannosylation, beta-trefoil, peptide binding protein |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Total number of polymer chains | 4 |
| Total formula weight | 97609.25 |
| Authors | Wild, K.,Chiapparino, A.,Hackmann, Y.,Mortensen, S.,Sinning, I. (deposition date: 2020-07-10, release date: 2020-12-23, Last modification date: 2024-01-31) |
| Primary citation | Chiapparino, A.,Grbavac, A.,Jonker, H.R.,Hackmann, Y.,Mortensen, S.,Zatorska, E.,Schott, A.,Stier, G.,Saxena, K.,Wild, K.,Schwalbe, H.,Strahl, S.,Sinning, I. Functional implications of MIR domains in protein O -mannosylation. Elife, 9:-, 2020 Cited by PubMed Abstract: Protein -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 -mannosylation. PubMed: 33357379DOI: 10.7554/eLife.61189 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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