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| | <StructureSection load='5tjo' size='340' side='right'caption='[[5tjo]], [[Resolution|resolution]] 1.57Å' scene=''> | | <StructureSection load='5tjo' size='340' side='right'caption='[[5tjo]], [[Resolution|resolution]] 1.57Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5tjo]] is a 1 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=5TJO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TJO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5tjo]] is a 1 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=5TJO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TJO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGB:alpha-L-Fucp-(1- 2)[alpha-D-Galp-(1- 3)]-beta-D-Galp-O(CH2)7CH3'>BGB</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</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]] 1.57Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5tjn|5tjn]], [[5tjk|5tjk]], [[5tjl|5tjl]], [[5tjm|5tjm]], [[5tjp|5tjp]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=HSH:OCTYL+BETA-D-GALACTOPYRANOSIDE'>HSH</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ABO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5tjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tjo OCA], [https://pdbe.org/5tjo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tjo RCSB], [https://www.ebi.ac.uk/pdbsum/5tjo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tjo ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5tjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tjo OCA], [http://pdbe.org/5tjo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tjo RCSB], [http://www.ebi.ac.uk/pdbsum/5tjo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tjo ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BGAT_HUMAN BGAT_HUMAN]] This protein is the basis of the ABO blood group system. The histo-blood group ABO involves three carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity that converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals lack such activity. | + | [https://www.uniprot.org/uniprot/BGAT_HUMAN BGAT_HUMAN] This protein is the basis of the ABO blood group system. The histo-blood group ABO involves three carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity that converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals lack such activity. |
| | <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: Evans, S V]] | + | [[Category: Evans SV]] |
| - | [[Category: Gagnon, S M.L]] | + | [[Category: Gagnon SML]] |
| - | [[Category: Legg, M S.G]] | + | [[Category: Legg MSG]] |
| - | [[Category: Glycosyltransferase]]
| + | |
| - | [[Category: Gt-a fold]]
| + | |
| - | [[Category: Histo blood group enzyme]]
| + | |
| - | [[Category: Product trisaccharide]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
BGAT_HUMAN This protein is the basis of the ABO blood group system. The histo-blood group ABO involves three carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity that converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals lack such activity.
Publication Abstract from PubMed
The human ABO(H) blood group A- and B-synthesizing glycosyltransferases GTA and GTB have been structurally characterized to high resolution in complex with their respective trisaccharide antigen products. These findings are particularly timely and relevant given the dearth of glycosyltransferase structures collected in complex with their saccharide reaction products. GTA and GTB utilize the same acceptor substrates, oligosaccharides terminating with alpha-l-Fucp-(1-->2)-beta-d-Galp-OR (where R is a glycolipid or glycoprotein), but use distinct UDP donor sugars, UDP-N-acetylgalactosamine and UDP-galactose, to generate the blood group A (alpha-l-Fucp-(1-->2)[alpha-d-GalNAcp-(1-->3)]-beta-d-Galp-OR) and blood group B (alpha-l-Fucp-(1-->2)[alpha-d-Galp-(1-->3)]-beta-d-Galp-OR) determinant structures, respectively. Structures of GTA and GTB in complex with their respective trisaccharide products reveal a conflict between the transferred sugar monosaccharide and the beta-phosphate of the UDP donor. Mapping of the binding epitopes by saturation transfer difference NMR measurements yielded data consistent with the X-ray structural results. Taken together these data suggest a mechanism of product release where monosaccharide transfer to the H-antigen acceptor induces active site disorder and ejection of the UDP leaving group prior to trisaccharide egress.
High-resolution crystal structures and STD NMR mapping of human ABO(H) blood group glycosyltransferases in complex with trisaccharide reaction products suggest a molecular basis for product release.,Gagnon SML, Legg MSG, Sindhuwinata N, Letts JA, Johal AR, Schuman B, Borisova SN, Palcic MM, Peters T, Evans SV Glycobiology. 2017 Oct 1;27(10):966-977. doi: 10.1093/glycob/cwx053. PMID:28575295[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gagnon SML, Legg MSG, Sindhuwinata N, Letts JA, Johal AR, Schuman B, Borisova SN, Palcic MM, Peters T, Evans SV. High-resolution crystal structures and STD NMR mapping of human ABO(H) blood group glycosyltransferases in complex with trisaccharide reaction products suggest a molecular basis for product release. Glycobiology. 2017 Oct 1;27(10):966-977. doi: 10.1093/glycob/cwx053. PMID:28575295 doi:http://dx.doi.org/10.1093/glycob/cwx053
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