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| | ==Crystal structure of catalytic domain of bovine beta1,4-galactosyltransferase mutant M344H-GalT1 complex with 6-sulfo-GlcNAc== | | ==Crystal structure of catalytic domain of bovine beta1,4-galactosyltransferase mutant M344H-GalT1 complex with 6-sulfo-GlcNAc== |
| - | <StructureSection load='4krv' size='340' side='right' caption='[[4krv]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='4krv' size='340' side='right'caption='[[4krv]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4krv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KRV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KRV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4krv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KRV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KRV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NGS:2-(ACETYLAMINO)-2-DEOXY-6-O-SULFO-BETA-D-GLUCOPYRANOSE'>NGS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDH:6-AMINOHEXYL-URIDINE-C1,5-DIPHOSPHATE'>UDH</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]] 2.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1tw5|1tw5]], [[4l41|4l41]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NGS:2-(ACETYLAMINO)-2-DEOXY-6-O-SULFO-BETA-D-GLUCOPYRANOSE'>NGS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDH:6-AMINOHEXYL-URIDINE-C1,5-DIPHOSPHATE'>UDH</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">B4GALT1, GALT, GGTB2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</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=4krv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4krv OCA], [https://pdbe.org/4krv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4krv RCSB], [https://www.ebi.ac.uk/pdbsum/4krv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4krv 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/Lactose_synthase Lactose synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.22 2.4.1.22] </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=4krv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4krv OCA], [http://pdbe.org/4krv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4krv RCSB], [http://www.ebi.ac.uk/pdbsum/4krv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4krv ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/B4GT1_BOVIN B4GT1_BOVIN]] The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix. | + | [https://www.uniprot.org/uniprot/B4GT1_BOVIN B4GT1_BOVIN] The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4krv" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4krv" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bovin]] | + | [[Category: Bos taurus]] |
| - | [[Category: Lactose synthase]] | + | [[Category: Large Structures]] |
| - | [[Category: Qasba, P K]] | + | [[Category: Qasba PK]] |
| - | [[Category: Ramakrishnan, B]] | + | [[Category: Ramakrishnan B]] |
| - | [[Category: Glycosyltransferase]]
| + | |
| - | [[Category: Golgi]]
| + | |
| - | [[Category: Gt-a fold]]
| + | |
| - | [[Category: Mutant enzyme]]
| + | |
| - | [[Category: N-acetyl-glucosamine]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Udp-galactose]]
| + | |
| Structural highlights
Function
B4GT1_BOVIN The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix.
Publication Abstract from PubMed
6-sulfate modified N-acetylglucosamine (6-sulfo-GlcNAc) is often found as part of many biologically important carbohydrate epitopes such as 6-sulfo-LeX. In these epitopes, the 6-sulfo-GlcNAc moiety is extended by a galactose sugar in a beta1-4 linkage. The beta4GalT1 enzyme transfers galactose (Gal) from UDP-Gal to N-acetylglucosamine (GlcNAc) in the presence of manganese. Here we report that the beta4GalT1 enzyme transfers Gal to the 6-sulfo-GlcNAc and 4-methylumbelliferyl-6-sulfo-N-acetyl-beta-D-glucosaminide (6-sulfo-betaGlcNAc-MU) acceptor substrates, although with very low efficiency. To understand the effect that the 6-sulfate group on the GlcNAc acceptor has on the catalytic activity of the beta4GalT1 molecule, we have determined the crystal structure of the catalytic domain of bovine beta4GalT1 mutant enzyme M344H-beta4GalT1 complex with the 6-sulfo-GlcNAc molecule. In the crystal structure, the 6-sulfo-GlcNAc is bound to the protein in a way that is similar to the GlcNAc molecule. However, the 6-sulfate group engages in additional interactions with the hydrophobic region, residues 276-285, of the protein molecule, and this group is found wedged between the aromatic side chains of Phe-280 and Trp314 residues. Since the side chain of the Trp314 residue undergoes conformational changes during the catalytic cycle of the enzyme, molecular interaction between Trp314 and the 6-sulfate group might hinder this conformational change. Therefore, the lack of a favorable binding environment, together with hindrance to the conformational changes, might be responsible for the poor catalytic activity.
Investigations on beta1,4-galactosyltransferase I using 6-sulfo-GlcNAc as an acceptor sugar substrate.,Ramakrishnan B, Moncrief AJ, Davis TA, Holland LA, Qasba PK Glycoconj J. 2013 Aug 13. PMID:23942731[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ramakrishnan B, Moncrief AJ, Davis TA, Holland LA, Qasba PK. Investigations on beta1,4-galactosyltransferase I using 6-sulfo-GlcNAc as an acceptor sugar substrate. Glycoconj J. 2013 Aug 13. PMID:23942731 doi:10.1007/s10719-013-9488-4
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