Structure of a double-domain phosphagen kinase reveals an asymmetric arrangement of the tandem domains
文献类型：期刊论文
| 作者 | Wang, ZM; Qiao, Z; Ye, S; Zhang, RG |
| 刊名 | ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
 |
| 出版日期 | 2015 |
| 卷号 | 71期号:1页码:779-789 |
| 关键词 | double-domain arginine kinase |
| 通讯作者 | Ye, S (reprint author), Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China.,yesheng@moon.ibp.ac.cn ; rzhang@ibp.ac.cn |
| 英文摘要 | Tandem duplications and fusions of single genes have led to magnificent expansions in the divergence of protein structures and functions over evolutionary timescales. One of the possible results is polydomain enzymes with interdomain cooperativities, few examples of which have been structurally characterized at the full-length level to explore their innate synergistic mechanisms. This work reports the crystal structures of a double-domain phosphagen kinase in both apo and ligand-bound states, revealing a novel asymmetric L-shaped arrangement of the two domains. Unexpectedly, the interdomain connections are not based on a flexible hinge linker but on a rigid secondary-structure element: a long alpha-helix that tethers the tandem domains in relatively fixed positions. Besides the connective helix, the two domains also contact each other directly and form an interdomain interface in which hydrogen bonds and hydrophobic interactions further stabilize the L-shaped domain arrangement. Molecular-dynamics simulations show that the interface is generally stable, suggesting that the asymmetric domain arrangement crystallographically observed in the present study is not a conformational state simply restrained by crystal-packing forces. It is possible that the asymmetrically arranged tandem domains could provide a structural basis for further studies of the interdomain synergy. |
| 学科主题 | Biochemistry & Molecular Biology; Biophysics; Crystallography |
| 类目[WOS] | Biochemical Research Methods ; Biochemistry & Molecular Biology ; Biophysics ; Crystallography |
| 关键词[WOS] | 2-DOMAIN ARGININE KINASE ; ANEMONE ANTHOPLEURA-JAPONICUS ; CRYSTAL-STRUCTURE ; MOLECULAR-DYNAMICS ; GENE DUPLICATION ; CREATINE-KINASE ; SUBSTRATE-FREE ; INDUCED FIT ; MECHANISM ; EVOLUTION |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000352507200005 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/117]  |
| 专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
| 推荐引用方式 GB/T 7714 | Wang, ZM,Qiao, Z,Ye, S,et al. Structure of a double-domain phosphagen kinase reveals an asymmetric arrangement of the tandem domains[J]. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY,2015,71(1):779-789. |
| APA | Wang, ZM,Qiao, Z,Ye, S,&Zhang, RG.(2015).Structure of a double-domain phosphagen kinase reveals an asymmetric arrangement of the tandem domains.ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY,71(1),779-789. |
| MLA | Wang, ZM,et al."Structure of a double-domain phosphagen kinase reveals an asymmetric arrangement of the tandem domains".ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 71.1(2015):779-789. |
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