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Carbohydrate-binding modules: fine-tuning polysaccharide recognition.
- A. Boraston, D. Bolam, H. Gilbert, G. Davies
- Chemistry, BiologyThe Biochemical journal
- 15 September 2004
The present review summarizes the impact structural biology has had on the understanding of the mechanisms by which CBMs bind to their target ligands.
Glycosyltransferases: structures, functions, and mechanisms.
- L. Lairson, B. Henrissat, G. Davies, S. Withers
- Biology, ChemistryAnnual review of biochemistry
- 2 June 2008
The expected two-step double-displacement mechanism is rendered less likely by the lack of conserved architecture in the region where a catalytic nucleophile would be expected, and a mechanism involving a short-lived oxocarbenium ion intermediate now seems the most likely, with the leaving phosphate serving as the base.
Structures and mechanisms of glycosyl hydrolases.
Structural and sequence-based classification of glycoside hydrolases.
An evolving hierarchical family classification for glycosyltransferases.
Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components
- R. Quinlan, Matthew D. Sweeney, P. Walton
- BiologyProceedings of the National Academy of Sciences
- 29 August 2011
It is demonstrated that copper is needed for GH61 maximal activity and that the formation of cellodextrin and oxidized cellodesxtrin products by GH61 is enhanced in the presence of small molecule redox-active cofactors such as ascorbate and gallate.
Structure of a flavonoid glucosyltransferase reveals the basis for plant natural product modification
The three‐dimensional structure of VvGT1 has been determined, both in its ‘Michaelis’ complex with a UDP‐glucose‐derived donor and the acceptor kaempferol and in complex with UDP and quercetin, providing the foundation for understanding the mechanism of these enzymes in small molecule homeostasis.
A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo.
Thiamet-G will find wide use in probing the functional role of O-GlcNAc in vertebrate brain, and it may also offer a route to blocking pathological hyperphosphorylation of tau in AD.
Crystal structure of an N-terminal fragment of the DNA gyrase B protein
The crystal structure of an N-terminal fragment of the Escherichia coli DNA gyrase B protein, com-plexed with a nonhn/drolysable ATP analogue, has been solved at 2.5 Å resolution. It consists of two…
Crystal structure of levansucrase from the Gram-negative bacterium Gluconacetobacter diazotrophicus.
- C. Martínez-Fleites, M. Ortiz-Lombardía, G. Davies
- Biology, EngineeringThe Biochemical journal
- 15 August 2005
A comparison of both structures, the mutagenesis data and the analysis of GH68 family multiple sequences alignment show a strong conservation of the sucrose hydrolytic machinery among levansucrases and also a structural equivalence of the Bs levanucrase Ca2+-binding site to the LsdA Cys339-Cys395 disulphide bridge, suggesting similar fold-stabilizing roles.