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- W3109479219 endingPage "100110" @default.
- W3109479219 startingPage "100110" @default.
- W3109479219 abstract "Poly-N-acetyl-lactosamine (poly-LacNAc) structures are composed of repeating [-Galβ(1,4)-GlcNAcβ(1,3)-]n glycan extensions. They are found on both N- and O-glycoproteins and glycolipids and play an important role in development, immune function, and human disease. The majority of mammalian poly-LacNAc is synthesized by the alternating iterative action of β1,3-N-acetylglucosaminyltransferase 2 (B3GNT2) and β1,4-galactosyltransferases. B3GNT2 is in the largest mammalian glycosyltransferase family, GT31, but little is known about the structure, substrate recognition, or catalysis by family members. Here we report the structures of human B3GNT2 in complex with UDP:Mg2+ and in complex with both UDP:Mg2+ and a glycan acceptor, lacto-N-neotetraose. The B3GNT2 structure conserves the GT-A fold and the DxD motif that coordinates a Mg2+ ion for binding the UDP-GlcNAc sugar donor. The acceptor complex shows interactions with only the terminal Galβ(1,4)-GlcNAcβ(1,3)- disaccharide unit, which likely explains the specificity for both N- and O-glycan acceptors. Modeling of the UDP-GlcNAc donor supports a direct displacement inverting catalytic mechanism. Comparative structural analysis indicates that nucleotide sugar donors for GT-A fold glycosyltransferases bind in similar positions and conformations without conserving interacting residues, even for enzymes that use the same donor substrate. In contrast, the B3GNT2 acceptor binding site is consistent with prior models suggesting that the evolution of acceptor specificity involves loops inserted into the stable GT-A fold. These observations support the hypothesis that GT-A fold glycosyltransferases employ coevolving donor, acceptor, and catalytic subsite modules as templates to achieve the complex diversity of glycan linkages in biological systems." @default.
- W3109479219 created "2020-12-07" @default.
- W3109479219 creator A5007660446 @default.
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- W3109479219 creator A5036497036 @default.
- W3109479219 creator A5055799923 @default.
- W3109479219 creator A5071655529 @default.
- W3109479219 date "2021-01-01" @default.
- W3109479219 modified "2023-10-16" @default.
- W3109479219 title "Comparison of human poly-N-acetyl-lactosamine synthase structure with GT-A fold glycosyltransferases supports a modular assembly of catalytic subsites" @default.
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- W3109479219 doi "https://doi.org/10.1074/jbc.ra120.015305" @default.
- W3109479219 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7948508" @default.
- W3109479219 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/33434582" @default.
- W3109479219 hasPublicationYear "2021" @default.
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