Toggle Main Menu Toggle Search

ePrints

Structural dissection and high-throughput screening of mannosylglycerate synthase

Lookup NU author(s): Dr James Flint, Dr David Bolam, Dr Louise Tailford, Professor Harry Gilbert

Downloads

Full text for this publication is not currently held within this repository. Alternative links are provided below where available.


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-α-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.


Publication metadata

Author(s): Flint J, Taylor E, Yang M, Bolam DN, Tailford L, Martinez-Fleites C, Dodson E, Davis B, Gilbert HJ, Davies G

Publication type: Article

Publication status: Published

Journal: Nature Structural and Molecular Biology

Year: 2005

Volume: 12

Issue: 7

Pages: 608-614

ISSN (print): 1545-9993

ISSN (electronic): 1545-9985

Publisher: Nature Publishing Group

URL: http://dx.doi.org/10.1038/nsmb950

DOI: 10.1038/nsmb950

PubMed id: 15951819


Altmetrics

Altmetrics provided by Altmetric


Actions

    Link to this publication


Share