@misc{oai:repo.qst.go.jp:00076123,
 author = {新井, 栄揮 and 柴崎, 千枝 and 清水, 瑠美 and 安達, 基泰 and 石橋, 松二郎 and 徳永, 廣子 and 徳永, 正雄 and Arai, Shigeki and Shibazaki, Chie and Shimizu, Rumi and Adachi, Motoyasu},
 month = {Jun},
 note = {Thioredoxin (TRX) is an important antioxidant to resist the oxidative stress. In this study, the structure of TRX from an extreme halophilic archaea Halobacterium NRC-1 (HsTRX-A, UniProtKB: O46709) having the highest acidic residue content [(D+E)/(K+R+H)=9.0] in the known TRXs was investigated to elucidate its haloadaptation mechanism. X-ray crystallographic analysis revealed that the structure of HsTRX-A was similar to those of the extant archaeal and non-halophilic TRXs (RMSDs for Cα atoms < 2.3 Å) and the resurrected Precambrian TRXs (RMSDs for Cα atoms < 1.5 Å) [1]. Although the structure of HsTRX-A was almost conserved throughout evolution, HsTRX-A has unique properties; e.g. the high density of negative charges (0.0035 Å-2) and the long hydrophilic N-terminal region (R1-D34), both of which improve the solubility of protein. Moreover, the water network formed by four water molecules was found near the active site residues (C47 and C50), which may assist the proton transfer at the active site residues under high salt environment. These observations will be helpful to understand the haloadaptation mechanism and molecular evolution of HsTRX-A. [1] Ingles-Prieto, A. et al. (2013) Structure, 21, 1690., 第19回日本蛋白質科学会年会・第71回日本細胞生物学会合同年次大会},
 title = {Haloadaptation mechanism and evolutional characteristics of  thioredoxin from Halobacterium NRC-1},
 year = {2019}
}