1gx0: Difference between revisions
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<StructureSection load='1gx0' size='340' side='right'caption='[[1gx0]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1gx0' size='340' side='right'caption='[[1gx0]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1gx0]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1gx0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GX0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GX0 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fg5|1fg5]], [[1g8o|1g8o]], [[1g93|1g93]], [[1gwv|1gwv]], [[1gww|1gww]], [[1gx4|1gx4]], [[1k4v|1k4v]], [[1o7o|1o7o]], [[1o7q|1o7q]], [[1o7r|1o7r]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fg5|1fg5]], [[1g8o|1g8o]], [[1g93|1g93]], [[1gwv|1gwv]], [[1gww|1gww]], [[1gx4|1gx4]], [[1k4v|1k4v]], [[1o7o|1o7o]], [[1o7q|1o7q]], [[1o7r|1o7r]]</div></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/N-acetyllactosaminide_3-alpha-galactosyltransferase N-acetyllactosaminide 3-alpha-galactosyltransferase], with EC number [https://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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gx0 OCA], [https://pdbe.org/1gx0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gx0 RCSB], [https://www.ebi.ac.uk/pdbsum/1gx0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gx0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/GGTA1_BOVIN GGTA1_BOVIN]] Transfer of galactose from UDP-galactose to an acceptor molecule (R). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 14:29, 28 July 2021
ALPHA-,1,3 GALACTOSYLTRANSFERASE - BETA-D-GALACTOSE COMPLEXALPHA-,1,3 GALACTOSYLTRANSFERASE - BETA-D-GALACTOSE COMPLEX
Structural highlights
Function[GGTA1_BOVIN] Transfer of galactose from UDP-galactose to an acceptor molecule (R). 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 PubMedBovine alpha-1,3-galactosyltransferase (alpha3GT) catalyzes the synthesis of the alpha-galactose (alpha-Gal) epitope, the target of natural human antibodies. It represents a family of enzymes, including the histo blood group A and B transferases, that catalyze retaining glycosyltransfer reactions of unknown mechanism. An initial study of alpha3GT in a crystal form with limited resolution and considerable disorder suggested the possible formation of a beta-galactosyl-enzyme covalent intermediate (Gastinel, L. N., Bignon, C., Misra, A. K., Hindsgaul, O., Shaper, J. H., and Joziasse, D. H. (2001) EMBO J. 20, 638-649). Highly ordered structures are described for complexes of alpha3GT with donor substrate, UDP-galactose, UDP- glucose, and two acceptor substrates, lactose and N-acetyllactosamine, at resolutions up to 1.46 A. Structural and calorimetric binding studies suggest an obligatory ordered binding of donor and acceptor substrates, linked to a donor substrate-induced conformational change, and the direct participation of UDP in acceptor binding. The monosaccharide-UDP bond is cleaved in the structures containing UDP-galactose and UDP-glucose, producing non-covalent complexes containing buried beta-galactose and alpha-glucose. The location of these monosaccharides and molecular modeling suggest that binding of a distorted conformation of UDP-galactose may be important in the catalytic mechanism of alpha3GT. Structural basis of ordered binding of donor and acceptor substrates to the retaining glycosyltransferase, alpha-1,3-galactosyltransferase.,Boix E, Zhang Y, Swaminathan GJ, Brew K, Acharya KR J Biol Chem. 2002 Aug 2;277(31):28310-8. Epub 2002 May 14. PMID:12011052[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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