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| <StructureSection load='6ry2' size='340' side='right'caption='[[6ry2]], [[Resolution|resolution]] 1.30Å' scene=''> | | <StructureSection load='6ry2' size='340' side='right'caption='[[6ry2]], [[Resolution|resolution]] 1.30Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6ry2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chatd Chatd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RY2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6RY2 FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RY2 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTHT_0020800 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=759272 CHATD])</td></tr>
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannan_endo-1,6-alpha-mannosidase Mannan endo-1,6-alpha-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.101 3.2.1.101] </span></td></tr>
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ry2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ry2 OCA], [https://pdbe.org/6ry2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ry2 RCSB], [https://www.ebi.ac.uk/pdbsum/6ry2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ry2 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=6ry2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ry2 OCA], [http://pdbe.org/6ry2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ry2 RCSB], [http://www.ebi.ac.uk/pdbsum/6ry2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ry2 ProSAT]</span></td></tr> | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| 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.
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| 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>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 6ry2" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Mannosidase 3D structures|Mannosidase 3D structures]] | | *[[Mannosidase 3D structures|Mannosidase 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Chatd]]
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Mannan endo-1,6-alpha-mannosidase]]
| | [[Category: Essen L-O]] |
| [[Category: Essen, L O]] | | [[Category: Vogt MS]] |
| [[Category: Vogt, M S]] | |
| [[Category: Fungal cell wall]]
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| [[Category: Gpi-anchor]]
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| [[Category: Gpi-cwp]]
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| [[Category: Hydrolase]]
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| [[Category: Plasma membrane]]
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| [[Category: Transglycosidase]]
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