1fg5
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==CRYSTAL STRUCTURE OF BOVINE ALPHA-1,3-GALACTOSYLTRANSFERASE CATALYTIC DOMAIN.== | ==CRYSTAL STRUCTURE OF BOVINE ALPHA-1,3-GALACTOSYLTRANSFERASE CATALYTIC DOMAIN.== | ||
| - | <StructureSection load='1fg5' size='340' side='right' caption='[[1fg5]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='1fg5' size='340' side='right'caption='[[1fg5]], [[Resolution|resolution]] 2.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1fg5]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1fg5]] is a 1 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=1FG5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FG5 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1fg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fg5 OCA], [https://pdbe.org/1fg5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fg5 RCSB], [https://www.ebi.ac.uk/pdbsum/1fg5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fg5 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]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fg5 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fg5 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | alpha1,3-galactosyltransferase (alpha3GalT, EC 2.4.1.151) is a Golgi-resident, type II transmembrane protein that transfers galactose from UDP-alpha-galactose to the terminal N:-acetyllactosamine unit of glycoconjugate glycans, producing the Galalpha1,3Galbeta1,4GlcNAc oligosaccharide structure present in most mammalian glycoproteins. Unlike most other mammals, humans and Old World primates do not possess alpha3GalT activity, which is relevant for the hyperacute rejection observed in pig-to-human xenotransplantation. The crystal structure of the catalytic domain of substrate-free bovine alpha3GalT, solved and refined to 2.3 A resolution, has a globular shape with an alpha/beta fold containing a narrow cleft on one face, and shares a UDP-binding domain (UBD) with the recently solved inverting glycosyltransferases. The substrate-bound complex, solved and refined to 2.5 A, allows the description of residues interacting directly with UDP-galactose. These structural data suggest that the strictly conserved residue E317 is likely to be the catalytic nucleophile involved in galactose transfer with retention of anomeric configuration as accomplished by this enzyme. Moreover, the alpha3GalT structure helps to identify amino acid residues that determine the specificities of the highly homologous ABO histo-blood group and glycosphingolipid glycosyltransferases. | ||
| - | + | ==See Also== | |
| - | + | *[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Bos taurus]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Bignon | + | [[Category: Bignon C]] |
| - | [[Category: Gastinel | + | [[Category: Gastinel LN]] |
| - | [[Category: Joziasse | + | [[Category: Joziasse DH]] |
| - | [[Category: Shaper | + | [[Category: Shaper JH]] |
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Current revision
CRYSTAL STRUCTURE OF BOVINE ALPHA-1,3-GALACTOSYLTRANSFERASE CATALYTIC DOMAIN.
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