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. Author manuscript; available in PMC: 2011 Oct 1.
Published in final edited form as: Curr Opin Struct Biol. 2010 Aug 11;20(5):536–542. doi: 10.1016/j.sbi.2010.07.004

Figure 1.

Figure 1

(a) The crystal structure of the bovine β4Gal-T1•Mn2+•UDP-GalNAc complex (pdb 1OQM) with a GlcNAc molecule modeled in the acceptor binding site. The UDP-GalNAc and GlcNAc molecules are shown in a ball and stick diagram. The side-chain hydroxyl group of Tyr289 residue forms a hydrogen bond (shown as black dotted line) with the carbonyl oxygen atom of the N-acetyl group of the GalNAc moiety. (b) Protein sequence comparison of the bovine β4Gal-T1 shown near the vicinity of the Y289 residues (black arrow), along with its homolog proteins from various species. Only in the vertebrate homolog proteins is the Y289 residue conversed as a Tyr residue, whereas in the invertebrates it is either Leu or Ile.