1OMX
Crystal structure of mouse alpha-1,4-N-acetylhexosaminyltransferase (EXTL2)
Summary for 1OMX
| Entry DOI | 10.2210/pdb1omx/pdb |
| Related | 1OMZ 1ON6 1ON8 |
| Descriptor | Alpha-1,4-N-acetylhexosaminyltransferase EXTL2, 1,2-ETHANEDIOL (3 entities in total) |
| Functional Keywords | dxd motif, rossmann fold, transferase |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Endoplasmic reticulum membrane ; Single-pass type II membrane protein : Q9ES89 |
| Total number of polymer chains | 2 |
| Total formula weight | 66978.83 |
| Authors | Pedersen, L.C.,Dong, J.,Taniguchi, F.,Kitagawa, H.,Krahn, J.M.,Pedersen, L.G.,Sugahara, K.,Negishi, M. (deposition date: 2003-02-26, release date: 2003-04-22, Last modification date: 2024-10-30) |
| Primary citation | Pedersen, L.C.,Dong, J.,Taniguchi, F.,Kitagawa, H.,Krahn, J.M.,Pedersen, L.G.,Sugahara, K.,Negishi, M. Crystal structure of an alpha-1,4-N-acetylhexosaminyltransferase (EXTL2), a member of the exostosin gene family involved in heparan sulfate biosynthesis J.Biol.Chem., 278:14420-14428, 2003 Cited by PubMed Abstract: EXTL2, 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. PubMed: 12562774DOI: 10.1074/jbc.M210532200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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