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==Crystal structure of mouse alpha-1,4-N-acetylhexosaminyltransferase (EXTL2)== | ==Crystal structure of mouse alpha-1,4-N-acetylhexosaminyltransferase (EXTL2)== | ||
<StructureSection load='1omx' size='340' side='right' caption='[[1omx]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='1omx' size='340' side='right' caption='[[1omx]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1omz|1omz]], [[1on6|1on6]], [[1on8|1on8]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1omz|1omz]], [[1on6|1on6]], [[1on8|1on8]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EXTL2 OR EXTR2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EXTL2 OR EXTR2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=1omx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1omx OCA], [http://pdbe.org/1omx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1omx RCSB], [http://www.ebi.ac.uk/pdbsum/1omx PDBsum]</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=1omx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1omx OCA], [http://pdbe.org/1omx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1omx RCSB], [http://www.ebi.ac.uk/pdbsum/1omx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1omx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == |
Revision as of 12:29, 12 October 2017
Crystal structure of mouse alpha-1,4-N-acetylhexosaminyltransferase (EXTL2)Crystal structure of mouse alpha-1,4-N-acetylhexosaminyltransferase (EXTL2)
Structural highlights
Function[EXTL2_MOUSE] Glycosyltransferase required for the biosynthesis of heparan-sulfate and responsible for the alternating addition of beta-1-4-linked glucuronic acid (GlcA) and alpha-1-4-linked N-acetylglucosamine (GlcNAc) units to nascent heparan sulfate chains (By similarity). 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 PubMedEXTL2, an alpha1,4-N-acetylhexosaminyltransferase, catalyzes the transfer reaction of N-acetylglucosamine and N-acetylgalactosamine from the respective UDP-sugars to the non-reducing end of [glucuronic acid]beta1-3[galactose]beta1-O-naphthalenemethanol, an acceptor substrate analog of the natural common linker of various glycosylaminoglycans. We have solved the x-ray crystal structure of the catalytic domain of mouse EXTL2 in the apo-form and with donor substrates UDP-N-acetylglucosamine and UDP-N-acetylgalactosamine. In addition, a structure of the ternary complex with UDP and the acceptor substrate analog [glucuronic acid]beta1-3[galactose]beta1-O-naphthalenemethanol has been determined. These structures reveal three highly conserved residues, Asn-243, Asp-246, and Arg-293, located at the active site. Mutation of these residues greatly decreases the activity. In the ternary complex, an interaction exists between the beta-phosphate of the UDP leaving group and the acceptor hydroxyl of the substrate that may play a functional role in catalysis. These structures represent the first structures from the exostosin gene family and provide important insight into the mechanisms of alpha1,4-N-acetylhexosaminyl transfer in heparan biosynthesis. Crystal structure of an alpha 1,4-N-acetylhexosaminyltransferase (EXTL2), a member of the exostosin gene family involved in heparan sulfate biosynthesis.,Pedersen LC, Dong J, Taniguchi F, Kitagawa H, Krahn JM, Pedersen LG, Sugahara K, Negishi M J Biol Chem. 2003 Apr 18;278(16):14420-8. Epub 2003 Jan 31. PMID:12562774[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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