3OC9

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

3OC9 の概要

• エントリーDOI: 10.2210/pdb3oc9/pdb
• 分子名称: UDP-N-acetylglucosamine pyrophosphorylase, SULFATE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: structural genomics, seattle structural genomics center for infectious disease, ssgcid, anaerobic parasitic protozoan, amoebic dysentery, amoebic liver abscess, cysts, udp-n-acetylglucosamine diphosphorylase, transferase, nucleotidyl transferase
• 由来する生物種: Entamoeba histolytica
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 46758.53

構造登録者

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2010-08-09, 公開日: 2010-08-18, 最終更新日: 2023-09-06)

主引用文献

Edwards, T.E.,Gardberg, A.S.,Phan, I.Q.,Zhang, Y.,Staker, B.L.,Myler, P.J.,Lorimer, D.D.
Structure of uridine diphosphate N-acetylglucosamine pyrophosphorylase from Entamoeba histolytica.
Acta Crystallogr F Struct Biol Commun, 71:560-565, 2015

PubMed Abstract: 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 Å 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 α-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.

PubMed: 25945709
DOI: 10.1107/S2053230X1500179X

実験手法

X-RAY DIFFRACTION (1.8 Å)