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Title 

Identification of a highly conserved hypothetical protein TON_0340 as a probable manganese-dependent phosphatase

Authors 

Y S SohnS G LeeK H LeeBonsu KuHo Chul ShinS S ChaY G KimH S LeeS G KangB H Oh

Publisher 

Public Library of Science

Issue Date 

2016

Citation 

Plos One, vol. 11, no. 12, pp. e0167549-e0167549

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

ISSN 

1932-6203

Link 

http://dx.doi.org/10.1371/journal.pone.0167549

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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