5GL4

Crystal structure of TON_0340 in complex with Mn

5GL4 の概要

• エントリーDOI: 10.2210/pdb5gl4/pdb
• 分子名称: Uncharacterized protein, MANGANESE (II) ION (3 entities in total)
• 機能のキーワード: ton_0340, thermococcus onnurineus, mn2+-dependent phosphatase, unknown function
• 由来する生物種: Thermococcus onnurineus (strain NA1)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 175579.13

構造登録者

Lee, S.G.,Sohn, Y.S.,Oh, B.H. (登録日: 2016-07-08, 公開日: 2016-12-14, 最終更新日: 2023-11-08)

主引用文献

Sohn, Y.S.,Lee, S.G.,Lee, K.H.,Ku, B.,Shin, H.C.,Cha, S.S.,Kim, Y.G.,Lee, H.S.,Kang, S.G.,Oh, B.H.
Identification of a Highly Conserved Hypothetical Protein TON_0340 as a Probable Manganese-Dependent Phosphatase.
PLoS ONE, 11:e0167549-e0167549, 2016

PubMed 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.

PubMed: 27907125
DOI: 10.1371/journal.pone.0167549

実験手法

X-RAY DIFFRACTION (2.2 Å)