@article{oai:repo.qst.go.jp:00049344,
 author = {柴崎, 千枝 and 新井, 栄揮 and 清水, 瑠美 and 佐伯, 盛久 and 木下, 誉富 (大阪府立大学 第5学系群 生物系) and Andreas, Ostermann(ドイツ FRMII) and Tobias, E. Schrader(ドイツ JCNS) and 黒崎, 譲 and 角南, 智子 and 黒木, 良太(JAEA) and 安達, 基泰 and Shibazaki, Chie and Arai, Shigeki and Shimizu, Rumi and Saeki, Morihisa and Kurosaki, Yuzuru and Sunami, Tomoko and Adachi, Motoyasu},
 issue = {24},
 journal = {Journal of Molecular Biology},
 month = {Dec},
 note = {Casein kinase 2 (CK2) is a eukaryotic serine-threonine protein kinase that forms a tetramer composed of two alpha and beta subunits.  CK2 has a broad phosphorylation activity against various regulatory proteins, which are important survival factors in eukaryotic cell.  In order to clarify the hydration structure and the catalytic mechanism of CK2, we determined a crystal structure of alpha subunit of human CK2 including hydrogen and deuterium atoms by the joint crystallographic analysis using 1.9 Å resolution neutron data and 1.1 Å resolution X-ray data. The analysis revealed the structures of conserved water molecule at the active site and a long hydrogen bonding network originating from the catalytic Asp156 which is well known to enhance the nucleophilicity of the substrate OH group to the -phospho group of ATP by elimination of proton.  His148 and highly conserved Asp214 in kinase family are located in the middle of the network.  The mutational analysis on His148 showed significant differences in turnover of catalysis with the similar affinity to ATP.  These findings shed new light on the catalytic mechanism of protein kinase, in which the hydrogen bond network through C-terminal domain enables the general base catalyst (Asp156) to relay a proton linking to the bulk solvent via intermediates of a pair of residues (His148 and Asp214).},
 pages = {5094--5104},
 title = {Hydration structures of the human protein kinase CK2α clarified by joint neutron and X-ray crystallography},
 volume = {430},
 year = {2018}
}