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Crystal structure of the Fucosylgalactoside alpha N-acetylgalactosaminyltransferase (GTA, cisAB mutant L266G, G268A)Crystal structure of the Fucosylgalactoside alpha N-acetylgalactosaminyltransferase (GTA, cisAB mutant L266G, G268A)
Structural highlights
Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedGlycosyltransferases are carbohydrate-active enzymes with essential roles in numerous important biological processes. We have developed a new donor analog for galactosyltransferases that locks a representative target enzyme in a catalytically inactive conformation, thus almost completely abolishing sugar transfer. Results with other galactosyltransferases suggest that this unique mode of glycosyltransferase inhibition may also be generally applicable to other members of this important enzyme family. Structural and mechanistic basis for a new mode of glycosyltransferase inhibition.,Pesnot T, Jorgensen R, Palcic MM, Wagner GK Nat Chem Biol. 2010 May;6(5):321-3. Epub 2010 Apr 4. PMID:20364127[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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