2BO7
DISSECTION OF MANNOSYLGLYCERATE SYNTHASE: AN ARCHETYPAL MANNOSYLTRANSFERASE
Summary for 2BO7
Entry DOI | 10.2210/pdb2bo7/pdb |
Related | 2BO4 2BO6 2BO8 |
Descriptor | MANNOSYLGLYCERATE SYNTHASE, GUANOSINE-5'-DIPHOSPHATE, COBALT (II) ION, ... (4 entities in total) |
Functional Keywords | transferase, catalysis, glycosyltransferase, mannose, stereoselectivity |
Biological source | RHODOTHERMUS MARINUS |
Total number of polymer chains | 10 |
Total formula weight | 466886.07 |
Authors | Flint, J.,Taylor, E.,Yang, M.,Bolam, D.N.,Tailford, L.E.,Martinez-Fleites, C.,Dodson, E.J.,Davis, B.G.,Gilbert, H.J.,Davies, G.J. (deposition date: 2005-04-08, release date: 2005-06-06, Last modification date: 2023-12-13) |
Primary citation | Flint, J.,Taylor, E.,Yang, M.,Bolam, D.N.,Tailford, L.E.,Martinez-Fleites, C.,Dodson, E.J.,Davis, B.G.,Gilbert, H.J.,Davies, G.J. Structural dissection and high-throughput screening of mannosylglycerate synthase. Nat. Struct. Mol. Biol., 12:608-614, 2005 Cited by PubMed Abstract: The enzymatic transfer of activated mannose yields mannosides in glycoconjugates and oligo- and polysaccharides. Yet, despite its biological necessity, the mechanism by which glycosyltransferases recognize mannose and catalyze its transfer to acceptor molecules is poorly understood. Here, we report broad high-throughput screening and kinetic analyses of both natural and synthetic substrates of Rhodothermus marinus mannosylglycerate synthase (MGS), which catalyzes the formation of the stress protectant 2-O-alpha-D-mannosyl glycerate. The sequence of MGS indicates that it is at the cusp of inverting and retaining transferases. The structures of apo MGS and complexes with donor and acceptor molecules, including GDP-mannose, combined with mutagenesis of the binding and catalytic sites, unveil the mannosyl transfer center. Nucleotide specificity is as important in GDP-D-mannose recognition as the nature of the donor sugar. PubMed: 15951819DOI: 10.1038/nsmb950 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.95 Å) |
Structure validation
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