3oc9
Crystal structure of putative UDP-N-acetylglucosamine pyrophosphorylase from Entamoeba histolyticaCrystal structure of putative UDP-N-acetylglucosamine pyrophosphorylase from Entamoeba histolytica
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedUridine diphosphate N-acetylglucosamine pyrophosphorylase (UAP) catalyzes the final step in the synthesis of UDP-GlcNAc, which is involved in cell-wall biogenesis in plants and fungi and in protein glycosylation. Small-molecule inhibitors have been developed against UAP from Trypanosoma brucei that target an allosteric pocket to provide selectivity over the human enzyme. A 1.8 A resolution crystal structure was determined of UAP from Entamoeba histolytica, an anaerobic parasitic protozoan that causes amoebic dysentery. Although E. histolytica UAP exhibits the same three-domain global architecture as other UAPs, it appears to lack three alpha-helices at the N-terminus and contains two amino acids in the allosteric pocket that make it appear more like the enzyme from the human host than that from the other parasite T. brucei. Thus, allosteric inhibitors of T. brucei UAP are unlikely to target Entamoeba UAPs. Structure of uridine diphosphate N-acetylglucosamine pyrophosphorylase from Entamoeba histolytica.,Edwards TE, Gardberg AS, Phan IQ, Zhang Y, Staker BL, Myler PJ, Lorimer DD Acta Crystallogr F Struct Biol Commun. 2015 May;71(Pt 5):560-5. doi:, 10.1107/S2053230X1500179X. Epub 2015 Apr 21. PMID:25945709[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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