1gx4

<StructureSection load='1gx4' size='340' side='right'caption='[[1gx4]], [[Resolution|resolution]] 1.46&Aring;' scene=''>

<table><tr><td colspan='2'>[[1gx4]] 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=1GX4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GX4 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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></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=1gx4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gx4 OCA], [http://pdbe.org/1gx4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gx4 RCSB], [http://www.ebi.ac.uk/pdbsum/1gx4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gx4 ProSAT]</span></td></tr>

== Function ==

[[http://www.uniprot.org/uniprot/GGTA1_BOVIN GGTA1_BOVIN]] Transfer of galactose from UDP-galactose to an acceptor molecule (R).

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Bovine 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<ref>PMID:12011052</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1gx4" style="background-color:#fffaf0;"></div>

*[[Glycosyltransferase|Glycosyltransferase]]

[[Category: Bovin]]

[[Category: Acharya, K R]]

[[Category: Boix, E]]

[[Category: Brew, K]]

[[Category: Swaminathan, G J]]

[[Category: Zhang, Y]]

[[Category: Transferase]]