3oc9 | pdb_00003oc9

Crystal structure of putative UDP-N-acetylglucosamine pyrophosphorylase from Entamoeba histolytica

spinqualitylabelsall models 3oc9, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3oc9 is a 1 chain structure with sequence from Entamoeba histolytica HM-1:IMSS. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: EDO, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C4M036_ENTH1 Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Uridine 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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