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| | ==Crystal Structure of Human N-acetylgalactosaminyltransferase (GTA) Complexed with H type I Trisaccharide== | | ==Crystal Structure of Human N-acetylgalactosaminyltransferase (GTA) Complexed with H type I Trisaccharide== |
| - | <StructureSection load='1zi5' size='340' side='right' caption='[[1zi5]], [[Resolution|resolution]] 1.55Å' scene=''> | + | <StructureSection load='1zi5' size='340' side='right'caption='[[1zi5]], [[Resolution|resolution]] 1.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1zi5]] 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=1ZI5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZI5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1zi5]] 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=1ZI5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZI5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DR3:6-DEOXY-ALPHA-L-GALACTOPYRANOSYL-(1- 2)-BETA-D-GALACTOPYRANOSYL-(1- 3)-2-(ACETYLAMINO)-2-DEOXY-BETA-D-GLUCOPYRANOSE'>DR3</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</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]] 1.55Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zhj|1zhj]], [[1zi1|1zi1]], [[1zi3|1zi3]], [[1zjo|1zjo]], [[1zi4|1zi4]], [[1ziz|1ziz]], [[1zj0|1zj0]], [[1zj1|1zj1]], [[1zj2|1zj2]], [[1zj3|1zj3]], [[1zjp|1zjp]]</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=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900049:H+type+1+antigen,+beta+anomer'>PRD_900049</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</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=1zi5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zi5 OCA], [https://pdbe.org/1zi5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zi5 RCSB], [https://www.ebi.ac.uk/pdbsum/1zi5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zi5 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycoprotein-fucosylgalactoside_alpha-N-acetylgalactosaminyltransferase Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.40 2.4.1.40] </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=1zi5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zi5 OCA], [http://pdbe.org/1zi5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zi5 RCSB], [http://www.ebi.ac.uk/pdbsum/1zi5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zi5 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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1zi5" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1zi5" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]] | + | [[Category: Large Structures]] |
| - | [[Category: Barry, C H]] | + | [[Category: Barry CH]] |
| - | [[Category: Borisova, S N]] | + | [[Category: Borisova SN]] |
| - | [[Category: Evans, S V]] | + | [[Category: Evans SV]] |
| - | [[Category: Fang, Y R]] | + | [[Category: Fang YR]] |
| - | [[Category: Letts, J A]] | + | [[Category: Letts JA]] |
| - | [[Category: Palcic, M M]] | + | [[Category: Palcic MM]] |
| - | [[Category: Rose, N L]] | + | [[Category: Rose NL]] |
| - | [[Category: Seto, N O]] | + | [[Category: Seto NO]] |
| - | [[Category: Blood group]]
| + | |
| - | [[Category: Glycosyltransferase]]
| + | |
| - | [[Category: Gta]]
| + | |
| - | [[Category: H-antigen]]
| + | |
| - | [[Category: Retaining]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
1zi5 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.55Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
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.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The human ABO(H) blood group A and B antigens are generated by the homologous glycosyltransferases A (GTA) and B (GTB), which add the monosaccharides GalNAc and Gal, respectively, to the cell-surface H antigens. In the first comprehensive structural study of the recognition by a glycosyltransferase of a panel of substrates corresponding to acceptor fragments, 14 high resolution crystal structures of GTA and GTB have been determined in the presence of oligosaccharides corresponding to different segments of the type I (alpha-l-Fucp-(1-->2)-beta-D-Galp-(1-->3)-beta-D-GlcNAcp-OR, where R is a glycoprotein or glycolipid in natural acceptors) and type II (alpha-l-Fucp-(1-->2)-beta-D-Galp-(1-->4)-beta-d-GlcNAcp-OR) H antigen trisaccharides. GTA and GTB differ in only four "critical" amino acid residues (Arg/Gly-176, Gly/Ser-235, Leu/Met-266, and Gly/Ala-268). As these enzymes both utilize the H antigen acceptors, the four critical residues had been thought to be involved strictly in donor recognition; however, we now report that acceptor binding and subsequent transfer are significantly influenced by two of these residues: Gly/Ser-235 and Leu/Met-266. Furthermore, these structures show that acceptor recognition is dominated by the central Gal residue despite the fact that the L-Fuc residue is required for efficient catalysis and give direct insight into the design of model inhibitors for GTA and GTB.
Differential recognition of the type I and II H antigen acceptors by the human ABO(H) blood group A and B glycosyltransferases.,Letts JA, Rose NL, Fang YR, Barry CH, Borisova SN, Seto NO, Palcic MM, Evans SV J Biol Chem. 2006 Feb 10;281(6):3625-32. Epub 2005 Dec 2. PMID:16326711[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Letts JA, Rose NL, Fang YR, Barry CH, Borisova SN, Seto NO, Palcic MM, Evans SV. Differential recognition of the type I and II H antigen acceptors by the human ABO(H) blood group A and B glycosyltransferases. J Biol Chem. 2006 Feb 10;281(6):3625-32. Epub 2005 Dec 2. PMID:16326711 doi:http://dx.doi.org/10.1074/jbc.M507620200
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