5f13
Structure of Mn bound DUF89 from Saccharomyces cerevisiaeStructure of Mn bound DUF89 from Saccharomyces cerevisiae
Structural highlights
FunctionARMT1_YEAST O-methyltransferase that methylates glutamate residues of target proteins to form gamma-glutamyl methyl ester residues.[UniProtKB:Q9H993] Publication Abstract from PubMedDUF89 family proteins occur widely in both prokaryotes and eukaryotes, but their functions are unknown. Here we define three DUF89 subfamilies (I, II, and III), with subfamily II being split into stand-alone proteins and proteins fused to pantothenate kinase (PanK). We demonstrated that DUF89 proteins have metal-dependent phosphatase activity against reactive phosphoesters or their damaged forms, notably sugar phosphates (subfamilies II and III), phosphopantetheine and its S-sulfonate or sulfonate (subfamily II-PanK fusions), and nucleotides (subfamily I). Genetic and comparative genomic data strongly associated DUF89 genes with phosphoester metabolism. The crystal structure of the yeast (Saccharomyces cerevisiae) subfamily III protein YMR027W revealed a novel phosphatase active site with fructose 6-phosphate and Mg2+ bound near conserved signature residues Asp254 and Asn255 that are critical for activity. These findings indicate that DUF89 proteins are previously unrecognized hydrolases whose characteristic in vivo function is to limit potentially harmful buildups of normal or damaged phosphometabolites. A family of metal-dependent phosphatases implicated in metabolite damage-control.,Huang L, Khusnutdinova A, Nocek B, Brown G, Xu X, Cui H, Petit P, Flick R, Zallot R, Balmant K, Ziemak MJ, Shanklin J, de Crecy-Lagard V, Fiehn O, Gregory JF 3rd, Joachimiak A, Savchenko A, Yakunin AF, Hanson AD Nat Chem Biol. 2016 Jun 20. doi: 10.1038/nchembio.2108. PMID:27322068[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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