Identification of a Highly Conserved Hypothetical Protein TON_0340 as a Probable Manganese-Dependent Phosphatase
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Title
- Identification of a Highly Conserved Hypothetical Protein TON_0340 as a Probable Manganese-Dependent Phosphatase
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Author(s)
- Sohn, Young-Sik; Lee, Seong-Gyu; Lee, Kwang-Hoon; Ku, Bonsu; Shine, Ho-Chul; Cha, Sun-Shin; Kim, Yeon-Gil; Lee, Hyun Sook; Kang, Sung-Gyun; Oh, Byung-Ha
- KIOST Author(s)
- Lee, Hyun Sook(이현숙); Kang, Sung Gyun(강성균)
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Alternative Author(s)
- 이현숙; 강성균
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Publication Year
- 2016-12-01
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Abstract
- A hypothetical protein TON_0340 of a Thermococcus species is a protein conserved in a variety of organisms including human. Herein, we present four different crystal structures of TON_0340, leading to the identification of an active-site cavity harboring a metal-binding site composed of six invariant aspartate and glutamate residues that coordinate one to three metal ions. Biochemical and mutational analyses involving many phosphorous compounds show that TON_0340 is a Mn2+-dependent phosphatase. Mg2+ binds to TON_0340 less tightly and activates the phosphatase activity less efficiently than Mn2+. Whereas Ca2+ and Zn2+ are able to bind to the protein, they are unable to activate its enzymatic activity. Since the active-site cavity is small and largely composed of nearly invariant stretches of 11 or 13 amino acids, the physiological substrates of TON_0340 and its homologues are likely to be a small and the same molecule. The Mn2+-bound TON_0340 structure provides a canonical model for the ubiquitously present TON_0340 homologues and lays a strong foundation for the elucidation of their substrate and biological function.
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ISSN
- 1932-6203
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URI
- https://sciwatch.kiost.ac.kr/handle/2020.kiost/1376
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DOI
- 10.1371/journal.pone.0167549
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Bibliographic Citation
- PLOS ONE, v.11, no.12, 2016
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Publisher
- PUBLIC LIBRARY SCIENCE
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Subject
- IB RIBONUCLEOTIDE REDUCTASE; N-OXYGENASE AURF; CRYSTAL-STRUCTURE; SEQUENCE; DNA
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Type
- Article
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Language
- English
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Document Type
- Article
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