Abstract
The vast majority of glycosidic-bond synthesis in nature is performed by glycosyltransferases, which use activated glycosides as the sugar donor. Typically, the activated leaving group is a nucleoside phosphate, lipid phosphate or phosphate. The nucleotide-sugar-dependent glycosyltransferases fall into over 50 sequence-based families, with the largest and most widespread family of inverting transferases named family GT-2. Here, we present the three-dimensional crystal structure of SpsA, the first and currently the only structural representative from family GT-2, in complex with both Mn-dTDP and Mg-dTDP at a resolution of 2 Angstrom. These structures reveal how SpsA and related enzymes may display nucleotide plasticity and permit a comparison of the catalytic centre of this enzyme with those from related sequence families whose three-dimensional structures have recently been determined. Family GT-2 enzymes, together with enzymes from families 7, 13 and 43, appear to form a clan of related structures with identical catalytic apparatus and reaction mechanism. (C) 2001 Academic Press.
| Original language | English |
|---|---|
| Pages (from-to) | 655-661 |
| Number of pages | 7 |
| Journal | Journal of Molecular Biology |
| Volume | 314 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - 7 Dec 2001 |
Keywords
- glycosyltransferase
- cellulose synthase
- catalysis
- inversion
- CRYSTAL-STRUCTURE
- GLYCOSIDE HYDROLASES
- BIOSYNTHESIS
- MECHANISM
- GLUCOSYLTRANSFERASE
- IDENTIFICATION
- TRANSFERASE
- CELLULOSE
- POLYSACCHARIDES
- CLASSIFICATION