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2ZUA

Crystal structure of nucleoside diphosphate kinase from Haloarcula quadrata

2ZUA の概要
エントリーDOI10.2210/pdb2zua/pdb
分子名称Nucleoside diphosphate kinase (2 entities in total)
機能のキーワードferredoxin fold, kpn loop, transferase, kinase
由来する生物種Haloarcula quadrata
細胞内の位置Cytoplasm (By similarity): Q401C5
タンパク質・核酸の鎖数4
化学式量合計78946.42
構造登録者
Ichimura, T.,Yamamura, A.,Ohtsuka, J.,Miyazono, K.,Okai, M.,Nagata, K.,Tanokura, M. (登録日: 2008-10-15, 公開日: 2009-08-25, 最終更新日: 2023-11-01)
主引用文献Yamamura, A.,Ichimura, T.,Kamekura, M.,Mizuki, T.,Usami, R.,Makino, T.,Ohtsuka, J.,Miyazono, K.,Okai, M.,Nagata, K.,Tanokura, M.
Molecular mechanism of distinct salt-dependent enzyme activity of two halophilic nucleoside diphosphate kinases
Biophys.J., 96:4692-4700, 2009
Cited by
PubMed Abstract: Nucleoside diphosphate kinases from haloarchaea Haloarcula quadrata (NDK-q) and H. sinaiiensis (NDK-s) are identical except for one out of 154 residues, i.e., Arg(31) in NDK-q and Cys(31) in NDK-s. However, the salt-dependent activity profiles of NDK-q and NDK-s are quite different: the optimal NaCl concentrations of NDK-q and NDK-s are 1 M and 2 M, respectively. We analyzed the relationships of the secondary, tertiary, and quaternary structures and NDK activity of these NDKs at various salt concentrations, and revealed that 1), NDK-q is present as a hexamer under a wide range of salt concentrations (0.2-4 M NaCl), whereas NDK-s is present as a hexamer at an NaCl concentration above 2 M and as a dimer at NaCl concentrations below 1 M; 2), dimeric NDK-s has lower activity than hexameric NDK-s; and 3), dimeric NDK-s has higher helicity than hexameric NDK-s. We also determined the crystal structure of hexameric NDK-q, and revealed that Arg(31) plays an important role in stabilizing the hexamer. Thus the substitution of Arg (as in NDK-q) to Cys (as in NDK-s) at position 31 destabilizes the hexameric assembly, and causes dissociation to less active dimers at low salt concentrations.
PubMed: 19486691
DOI: 10.1016/j.bpj.2009.03.012
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.59 Å)
構造検証レポート
Validation report summary of 2zua
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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