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| | <StructureSection load='5nqa' size='340' side='right'caption='[[5nqa]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='5nqa' size='340' side='right'caption='[[5nqa]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5nqa]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NQA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5NQA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5nqa]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NQA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NQA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NGA:N-ACETYL-D-GALACTOSAMINE'>NGA</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]] 1.9Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GALNT4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NGA:N-ACETYL-D-GALACTOSAMINE'>NGA</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Polypeptide_N-acetylgalactosaminyltransferase Polypeptide N-acetylgalactosaminyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.41 2.4.1.41] </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=5nqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nqa OCA], [https://pdbe.org/5nqa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nqa RCSB], [https://www.ebi.ac.uk/pdbsum/5nqa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nqa 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=5nqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nqa OCA], [http://pdbe.org/5nqa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nqa RCSB], [http://www.ebi.ac.uk/pdbsum/5nqa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nqa ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GALT4_HUMAN GALT4_HUMAN]] Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a highest activity toward Muc7, EA2 and Muc2, with a lowest activity than GALNT2. Glycosylates 'Thr-57' of SELPLG. | + | [https://www.uniprot.org/uniprot/GALT4_HUMAN GALT4_HUMAN] Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a highest activity toward Muc7, EA2 and Muc2, with a lowest activity than GALNT2. Glycosylates 'Thr-57' of SELPLG. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Polypeptide N-acetylgalactosaminyltransferase]]
| + | [[Category: Clausen H]] |
| - | [[Category: Clausen, H]] | + | [[Category: Coelho H]] |
| - | [[Category: Coelho, H]] | + | [[Category: Companon I]] |
| - | [[Category: Companon, I]] | + | [[Category: Corzana F]] |
| - | [[Category: Corzana, F]] | + | [[Category: Daniel EJP]] |
| - | [[Category: Daniel, E J.P]] | + | [[Category: Diniz A]] |
| - | [[Category: Diniz, A]] | + | [[Category: Gerken TA]] |
| - | [[Category: Gerken, T A]] | + | [[Category: Hurtado-Guerrero R]] |
| - | [[Category: Hurtado-Guerrero, R]] | + | [[Category: Jimenez-Barbero J]] |
| - | [[Category: Jimenez-Barbero, J]] | + | [[Category: Jimenez-Oses G]] |
| - | [[Category: Jimenez-Oses, G]] | + | [[Category: Lira-Navarrete E]] |
| - | [[Category: Lira-Navarrete, E]] | + | [[Category: Marcelo F]] |
| - | [[Category: Marcelo, F]] | + | [[Category: Peregrina JM]] |
| - | [[Category: Peregrina, J M]] | + | [[Category: De las Rivas M]] |
| - | [[Category: Rivas, M de las]] | + | |
| - | [[Category: Chimera]]
| + | |
| - | [[Category: Flexible linker]]
| + | |
| - | [[Category: Galnac-t2]]
| + | |
| - | [[Category: Galnac-t4]]
| + | |
| - | [[Category: Glycosylation preference]]
| + | |
| - | [[Category: Std-nmr]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
GALT4_HUMAN Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a highest activity toward Muc7, EA2 and Muc2, with a lowest activity than GALNT2. Glycosylates 'Thr-57' of SELPLG.
Publication Abstract from PubMed
The polypeptide GalNAc-transferases (GalNAc-Ts), that initiate mucin-type O-glycosylation, consist of a catalytic and a lectin domain connected by a flexible linker. In addition to recognizing polypeptide sequence, the GalNAc-Ts exhibit unique long-range N- and/or C-terminal prior glycosylation (GalNAc-O-Ser/Thr) preferences modulated by the lectin domain. Here we report studies on GalNAc-T4 that reveal the origins of its unique N-terminal long-range glycopeptide specificity, which is the opposite of GalNAc-T2. The GalNAc-T4 structure bound to a monoglycopeptide shows that the GalNAc-binding site of its lectin domain is rotated relative to the homologous GalNAc-T2 structure, explaining their different long-range preferences. Kinetics and molecular dynamics simulations on several GalNAc-T2 flexible linker constructs show altered remote prior glycosylation preferences, confirming that the flexible linker dictates the rotation of the lectin domain, thus modulating the GalNAc-Ts' long-range preferences. This work for the first time provides the structural basis for the different remote prior glycosylation preferences of the GalNAc-Ts.
The interdomain flexible linker of the polypeptide GalNAc transferases dictates their long-range glycosylation preferences.,Rivas ML, Lira-Navarrete E, Daniel EJP, Companon I, Coelho H, Diniz A, Jimenez-Barbero J, Peregrina JM, Clausen H, Corzana F, Marcelo F, Jimenez-Oses G, Gerken TA, Hurtado-Guerrero R Nat Commun. 2017 Dec 5;8(1):1959. doi: 10.1038/s41467-017-02006-0. PMID:29208955[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rivas ML, Lira-Navarrete E, Daniel EJP, Companon I, Coelho H, Diniz A, Jimenez-Barbero J, Peregrina JM, Clausen H, Corzana F, Marcelo F, Jimenez-Oses G, Gerken TA, Hurtado-Guerrero R. The interdomain flexible linker of the polypeptide GalNAc transferases dictates their long-range glycosylation preferences. Nat Commun. 2017 Dec 5;8(1):1959. doi: 10.1038/s41467-017-02006-0. PMID:29208955 doi:http://dx.doi.org/10.1038/s41467-017-02006-0
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