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Hydration structures of the human protein kinase CK2α clarified by joint neutron and X-ray crystallography
https://repo.qst.go.jp/records/49344
https://repo.qst.go.jp/records/49344e2aabfb5-4851-4474-986e-b7215ed8e9fa
| Item type | 学術雑誌論文 / Journal Article(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2018-12-13 | |||||
| タイトル | ||||||
| タイトル | Hydration structures of the human protein kinase CK2α clarified by joint neutron and X-ray crystallography | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
| 資源タイプ | journal article | |||||
| アクセス権 | ||||||
| アクセス権 | metadata only access | |||||
| アクセス権URI | http://purl.org/coar/access_right/c_14cb | |||||
| 著者 |
柴崎, 千枝
× 柴崎, 千枝× 新井, 栄揮× 清水, 瑠美× 佐伯, 盛久× 木下, 誉富 (大阪府立大学 第5学系群 生物系)× Andreas, Ostermann(ドイツ FRMII)× Tobias, E. Schrader(ドイツ JCNS)× 黒崎, 譲× 角南, 智子× 黒木, 良太(JAEA)× 安達, 基泰× Shibazaki, Chie× Arai, Shigeki× Shimizu, Rumi× Saeki, Morihisa× Kurosaki, Yuzuru× Sunami, Tomoko× Adachi, Motoyasu |
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| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | 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). | |||||
| 書誌情報 |
Journal of Molecular Biology 巻 430, 号 24, p. 5094-5104, 発行日 2018-12 |
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| 出版者 | ||||||
| 出版者 | ELSEVIER | |||||
| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 0022-2836 | |||||
| DOI | ||||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | 10.1016/j.jmb.2018.09.018 | |||||
