1on6

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spinqualitylabelsall models 1on6, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of mouse alpha-1,4-N-acetylhexosaminotransferase (EXTL2) in complex with UDPGlcNAc

Overview

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.

About this Structure

1ON6 is a Single protein structure of sequence from Mus musculus with MN, UD1 and EDO as ligands. Full crystallographic information is available from OCA.

Reference

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

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