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2BO6

DISSECTION OF MANNOSYLGLYCERATE SYNTHASE: AN ARCHETYPAL MANNOSYLTRANSFERASE

Summary for 2BO6
Entry DOI10.2210/pdb2bo6/pdb
Related2BO4 2BO7 2BO8
DescriptorMANNOSYLGLYCERATE SYNTHASE, (2R)-2,3-DIHYDROXYPROPANOIC ACID, MANGANESE (II) ION, ... (4 entities in total)
Functional Keywordscatalysis, glycosyltransferase, mannose, transferase, stereoselectivity
Biological sourceRHODOTHERMUS MARINUS
Total number of polymer chains2
Total formula weight92694.98
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: 2024-05-08)
Primary citationFlint, 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 Mannosylglyceerate Synthase
Nat.Struct.Mol.Biol., 12:608-, 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: 15951819
DOI: 10.1038/NSMB950
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.45 Å)
Structure validation

226707

數據於2024-10-30公開中

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