6ry6: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ry6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ry6 OCA], [http://pdbe.org/6ry6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ry6 RCSB], [http://www.ebi.ac.uk/pdbsum/6ry6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ry6 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ry6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ry6 OCA], [http://pdbe.org/6ry6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ry6 RCSB], [http://www.ebi.ac.uk/pdbsum/6ry6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ry6 ProSAT]</span></td></tr> | ||
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== Publication Abstract from PubMed == | |||
The correct distribution and trafficking of proteins are essential for all organisms. Eukaryotes evolved a sophisticated trafficking system which allows proteins to reach their destination within highly compartmentalized cells. One eukaryotic hallmark is the attachment of a glycosylphosphatidylinositol (GPI) anchor to C-terminal omega-peptides, which are used as a zip code to guide a subset of membrane-anchored proteins through the secretory pathway to the plasma membrane. In fungi, the final destination of many GPI-anchored proteins is their outermost compartment, the cell wall. Enzymes of the Dfg5 subfamily catalyze the essential transfer of GPI-anchored substrates from the plasma membrane to the cell wall and discriminate between plasma membrane-resident GPI-anchored proteins and those transferred to the cell wall (GPI-CWP). We solved the structure of Dfg5 from a filamentous fungus and used in crystallo glycan fragment screening to reassemble the GPI-core glycan in a U-shaped conformation within its binding pocket. The resulting model of the membrane-bound Dfg5*GPI-CWP complex is validated by molecular dynamics (MD) simulations and in vivo mutants in yeast. The latter show that impaired transfer of GPI-CWPs causes distorted cell-wall integrity as indicated by increased chitin levels. The structure of a Dfg5*beta1,3-glycoside complex predicts transfer of GPI-CWP toward the nonreducing ends of acceptor glycans in the cell wall. In addition to our molecular model for Dfg5-mediated transglycosylation, we provide a rationale for how GPI-CWPs are specifically sorted toward the cell wall by using GPI-core glycan modifications. | |||
Structural base for the transfer of GPI-anchored glycoproteins into fungal cell walls.,Vogt MS, Schmitz GF, Varon Silva D, Mosch HU, Essen LO Proc Natl Acad Sci U S A. 2020 Sep 8;117(36):22061-22067. doi:, 10.1073/pnas.2010661117. Epub 2020 Aug 24. PMID:32839341<ref>PMID:32839341</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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==See Also== | |||
*[[Mannosidase 3D structures|Mannosidase 3D structures]] | |||
== References == | |||
<references/> | |||
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</StructureSection> | </StructureSection> | ||