DC Field | Value | Language |
---|---|---|
dc.contributor.author | Sohn, Young Sik | ko |
dc.contributor.author | Lee, Seong Gyu | ko |
dc.contributor.author | Lee, Kwang-Hoon | ko |
dc.contributor.author | Ku, Bonsu | ko |
dc.contributor.author | Shine, Ho-Chul | ko |
dc.contributor.author | Cha, Sun-Shin | ko |
dc.contributor.author | Kim, Yeon-Gil | ko |
dc.contributor.author | Lee, Hyun Sook | ko |
dc.contributor.author | Kang, Sung-Gyun | ko |
dc.contributor.author | Oh, Byung-Ha | ko |
dc.date.accessioned | 2017-01-09T08:08:24Z | - |
dc.date.available | 2017-01-09T08:08:24Z | - |
dc.date.created | 2017-01-09 | - |
dc.date.created | 2017-01-09 | - |
dc.date.issued | 2016-12 | - |
dc.identifier.citation | PLOS ONE, v.11, no.12 | - |
dc.identifier.issn | 1932-6203 | - |
dc.identifier.uri | http://hdl.handle.net/10203/216130 | - |
dc.description.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. | - |
dc.language | English | - |
dc.publisher | PUBLIC LIBRARY SCIENCE | - |
dc.subject | IB RIBONUCLEOTIDE REDUCTASE | - |
dc.subject | N-OXYGENASE AURF | - |
dc.subject | CRYSTAL-STRUCTURE | - |
dc.subject | SEQUENCE | - |
dc.subject | DNA | - |
dc.title | Identification of a Highly Conserved Hypothetical Protein TON_0340 as a Probable Manganese-Dependent Phosphatase | - |
dc.type | Article | - |
dc.identifier.wosid | 000389482700189 | - |
dc.identifier.scopusid | 2-s2.0-85000645675 | - |
dc.type.rims | ART | - |
dc.citation.volume | 11 | - |
dc.citation.issue | 12 | - |
dc.citation.publicationname | PLOS ONE | - |
dc.identifier.doi | 10.1371/journal.pone.0167549 | - |
dc.embargo.liftdate | 9999-12-31 | - |
dc.embargo.terms | 9999-12-31 | - |
dc.contributor.localauthor | Oh, Byung-Ha | - |
dc.contributor.nonIdAuthor | Lee, Kwang-Hoon | - |
dc.contributor.nonIdAuthor | Ku, Bonsu | - |
dc.contributor.nonIdAuthor | Shine, Ho-Chul | - |
dc.contributor.nonIdAuthor | Cha, Sun-Shin | - |
dc.contributor.nonIdAuthor | Kim, Yeon-Gil | - |
dc.contributor.nonIdAuthor | Lee, Hyun Sook | - |
dc.contributor.nonIdAuthor | Kang, Sung-Gyun | - |
dc.description.isOpenAccess | Y | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | IB RIBONUCLEOTIDE REDUCTASE | - |
dc.subject.keywordPlus | N-OXYGENASE AURF | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | SEQUENCE | - |
dc.subject.keywordPlus | DNA | - |
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