|
|
| Line 1: |
Line 1: |
| | | | |
| | ==A Native Ternary Complex of Alpha-1,3-Galactosyltransferase (a-3GalT) Supports a Conserved Reaction Mechanism for Retaining Glycosyltransferases - alpha-3GalT in complex with Co2+, UDP-Gal and lactose - a3GalT-Co2+-UDP-Gal-LAT-1== | | ==A Native Ternary Complex of Alpha-1,3-Galactosyltransferase (a-3GalT) Supports a Conserved Reaction Mechanism for Retaining Glycosyltransferases - alpha-3GalT in complex with Co2+, UDP-Gal and lactose - a3GalT-Co2+-UDP-Gal-LAT-1== |
| - | <StructureSection load='5nrb' size='340' side='right' caption='[[5nrb]], [[Resolution|resolution]] 2.24Å' scene=''> | + | <StructureSection load='5nrb' size='340' side='right'caption='[[5nrb]], [[Resolution|resolution]] 2.24Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5nrb]] 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=5NRB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NRB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5nrb]] 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=5NRB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NRB FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GDU:GALACTOSE-URIDINE-5-DIPHOSPHATE'>GDU</scene>, <scene name='pdbligand=LAT:BETA-LACTOSE'>LAT</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]] 2.24Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GGTA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GDU:GALACTOSE-URIDINE-5-DIPHOSPHATE'>GDU</scene>, <scene name='pdbligand=PRD_900004:beta-lactose'>PRD_900004</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetyllactosaminide_3-alpha-galactosyltransferase N-acetyllactosaminide 3-alpha-galactosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.87 2.4.1.87] </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=5nrb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nrb OCA], [https://pdbe.org/5nrb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nrb RCSB], [https://www.ebi.ac.uk/pdbsum/5nrb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nrb 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=5nrb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nrb OCA], [http://pdbe.org/5nrb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nrb RCSB], [http://www.ebi.ac.uk/pdbsum/5nrb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nrb ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GGTA1_BOVIN GGTA1_BOVIN]] Transfer of galactose from UDP-galactose to an acceptor molecule (R). | + | [https://www.uniprot.org/uniprot/GGTA1_BOVIN GGTA1_BOVIN] Transfer of galactose from UDP-galactose to an acceptor molecule (R). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 24: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bovin]] | + | [[Category: Bos taurus]] |
| - | [[Category: N-acetyllactosaminide 3-alpha-galactosyltransferase]] | + | [[Category: Large Structures]] |
| - | [[Category: Albesa-Jove, D]] | + | [[Category: Albesa-Jove D]] |
| - | [[Category: Guerin, M E]] | + | [[Category: Guerin ME]] |
| - | [[Category: Marina, A]] | + | [[Category: Marina A]] |
| - | [[Category: Sainz-Polo, M A]] | + | [[Category: Sainz-Polo MA]] |
| - | [[Category: Glycosyltransferase]]
| + | |
| - | [[Category: Gta]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
5nrb is a 2 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.24Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
GGTA1_BOVIN Transfer of galactose from UDP-galactose to an acceptor molecule (R).
Publication Abstract from PubMed
Glycosyltransferases (GTs) are a key family of enzymes that catalyses the synthesis of glycosidic bonds in all living organisms. The reaction involves the transfer of a glycosyl moiety and can proceed with retention or inversion of the anomeric configuration. To date, the elucidation of the catalytic mechanism of retaining GTs is of great controversy, particularly for those enzymes containing a putative nucleophilic residue in the active site, for which a double-displacement mechanism has been suggested. Here, we report native ternary complexes of the retaining alpha1,3-Galactosyltransferase (alpha3GalT) from Bos taurus - containing such a nucleophile in the active site - in a productive mode for catalysis, in the presence of its sugar donor UDP-Gal, the acceptor substrate lactose, and the divalent cation cofactor. This new experimental evidence supports a front-side substrate-assisted SNi-type reaction for alpha3GalT, and suggests a conserved common catalytic mechanism among retaining GTs.
Structural Snapshots of the Reaction Center of Family GT6 alpha1,3-Galactosyltransferase with Native Substrates. Insights into the Catalytic Mechanism of Retaining Glycosyltransferases.,Guerin ME, Albesa-Jove D, Sainz-Polo MA, Marina A Angew Chem Int Ed Engl. 2017 Sep 28. doi: 10.1002/anie.201707922. PMID:28960760[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Guerin ME, Albesa-Jove D, Sainz-Polo MA, Marina A. Structural Snapshots of the Reaction Center of Family GT6 alpha1,3-Galactosyltransferase with Native Substrates. Insights into the Catalytic Mechanism of Retaining Glycosyltransferases. Angew Chem Int Ed Engl. 2017 Sep 28. doi: 10.1002/anie.201707922. PMID:28960760 doi:http://dx.doi.org/10.1002/anie.201707922
|
