| Crystal structure of dna gyrase b ' domain sheds lights on the mechanism for t-segment navigation | |
| Fu, Guangsen1,2; Wu, Jinjun2,3; Liu, Wei4; Zhu, Deyu1,2; Hu, Yonglin1; Deng, Jiaoyu3; Zhang, Xian-En3; Bi, Lijun1; Wang, Da-Cheng1 | |
| 刊名 | Nucleic acids research
 |
| 2009-09-01 | |
| 卷号 | 37期号:17页码:5908-5916 |
| ISSN号 | 0305-1048 |
| DOI | 10.1093/nar/gkp586 |
| 通讯作者 | Bi, lijun(blj@sun5.ibp.ac.cn) |
| 英文摘要 | Dna gyrase is an indispensible marvelous molecular machine in manipulating the dna topology for the prokaryotes. in the 'two-gate' mechanism of dna topoisomerase, t-segment navigation from n- to dna-gate is a critical step, but the structural basis supporting this scheme is unclear. the crystal structure of dna gyrase b' subfragment from mycobacterium tuberculosis reveals an intrinsic homodimer. the two subunits, each consisting of a tail and a toprim domain, are tightly packed one another to form a 'crab-like' organization never observed previously from yeast topo ii. structural comparisons show two orientational alterations of the tail domain, which may be dominated by a 43-residue peptide at the b' module c-terminus. a highly conserved pentapeptide mediates large-scale intrasubunit conformational change as a hinge point. mutational studies highlight the significant roles of a negatively charge cluster on a groove at dimer interface. on the basis of structural analysis and mutation experiments, a sluice-like model for t-segment transport is proposed. |
| WOS关键词 | ARCHAEON SULFOLOBUS-SHIBATAE ; N-TERMINAL FRAGMENT ; X-RAY-SCATTERING ; ESCHERICHIA-COLI ; TOPOISOMERASE-II ; A SUBUNIT ; BINDING ; VI ; IA ; IDENTIFICATION |
| WOS研究方向 | Biochemistry & Molecular Biology |
| WOS类目 | Biochemistry & Molecular Biology |
| 语种 | 英语 |
| 出版者 | OXFORD UNIV PRESS |
| WOS记录号 | WOS:000271569100030 |
| 内容类型 | 期刊论文 |
| URI标识 | http://www.corc.org.cn/handle/1471x/2375539 |
| 专题 | 武汉病毒研究所 |
| 通讯作者 | Bi, Lijun |
| 作者单位 | 1.Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China 2.Chinese Acad Sci, Grad Univ, Beijing 100039, Peoples R China 3.Chinese Acad Sci, Wuhan Inst Virol, State Key Lab Virol, Wuhan 430071, Peoples R China 4.Karolinska Inst, Novum, Dept Biosci & Nutr, Ctr Struct Biochem, S-14157 Huddinge, Sweden |
| 推荐引用方式 GB/T 7714 | Fu, Guangsen,Wu, Jinjun,Liu, Wei,et al. Crystal structure of dna gyrase b ' domain sheds lights on the mechanism for t-segment navigation[J]. Nucleic acids research,2009,37(17):5908-5916. |
| APA | Fu, Guangsen.,Wu, Jinjun.,Liu, Wei.,Zhu, Deyu.,Hu, Yonglin.,...&Wang, Da-Cheng.(2009).Crystal structure of dna gyrase b ' domain sheds lights on the mechanism for t-segment navigation.Nucleic acids research,37(17),5908-5916. |
| MLA | Fu, Guangsen,et al."Crystal structure of dna gyrase b ' domain sheds lights on the mechanism for t-segment navigation".Nucleic acids research 37.17(2009):5908-5916. |
| 个性服务 |
| 查看访问统计 |
| 相关权益政策 |
| 暂无数据 |
| 收藏/分享 |
除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。
修改评论