Large conformation shifts of Vibrio cholerae VqmA dimer in the absence of target DNA provide insight into DNA-binding mechanisms of LuxR-type receptors
文献类型：期刊论文
| 作者 | Wu, H; Li, MJ; Peng, C; Yin, Y; Guo, HJ; Wang, WW; Xu, Q; Zhou, H; Xu, CY; Yu, F |
| 刊名 | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
 |
| 出版日期 | 2019 |
| 卷号 | 520期号:2页码:399-405 |
| 关键词 | TO-CELL COMMUNICATION CRYSTAL-STRUCTURE QUORUM AUTOINDUCER EXPRESSION REGULATOR |
| ISSN号 | 0006-291X |
| DOI | 10.1016/j.bbrc.2019.10.063 |
| 文献子类 | 期刊论文 |
| 英文摘要 | Quorum sensing regulates the biofilm formation and expression of virulence factors in Vibrio cholerae, an obligate human pathogen that continues to imperil human health. Cytoplasmic transcription factor VqmA is a LuxR-type receptor ubiquitous in the Vibrio genus and one vibriophage VP882 and plays an important role in V. cholerae pathogenicity. Here we presented the X-ray crystal structure of V. cholerae VqmA-DPO complex and compared it with the previously determined VqmA-DPO-DNA complex. To our knowledge, this is the first report on the crystal structures of the same LuxR-type receptor with two conformations of binding to DNA and not binding to DNA. Based on the results of structural analysis and biochemical assays, we revealed the secondary structure of the linker region between two function domains changed significantly, and DNA binding domains were covalently linked by a disulfide bond formed by the highly conserved Cys134. Besides, the distance between two DBD monomers became longer than that in DNA-binding conformation, and two alpha 8 helixes underwent a large conformation shift. The results of the structure-function analyses presented here improve our understanding of the complex mechanisms in the conformational changes of LuxR-type receptors caused by DNA binding. (C) 2019 Elsevier Inc. All rights reserved. |
| 语种 | 英语 |
| 源URL | [http://ir.sinap.ac.cn/handle/331007/32113]  |
| 专题 | 上海应用物理研究所_中科院上海应用物理研究所2011-2017年 |
| 作者单位 | 1.Chinese Acad Sci, Shanghai Inst Appl Phys, Shanghai 201800, Peoples R China; 2.Chinese Acad Sci, Shanghai Sci Res Ctr, Shanghai 201204, Peoples R China 3.Zhangjiang Lab, Natl Facil Prot Sci Shanghai, Shanghai 201210, Peoples R China; 4.Chinese Acad Sci, Shanghai Adv Res Inst, Shanghai 201204, Peoples R China; 5.Univ Chinese Acad Sci, Beijing 100049, Peoples R China; |
| 推荐引用方式 GB/T 7714 | Wu, H,Li, MJ,Peng, C,et al. Large conformation shifts of Vibrio cholerae VqmA dimer in the absence of target DNA provide insight into DNA-binding mechanisms of LuxR-type receptors[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,2019,520(2):399-405. |
| APA | Wu, H.,Li, MJ.,Peng, C.,Yin, Y.,Guo, HJ.,...&He, JH.(2019).Large conformation shifts of Vibrio cholerae VqmA dimer in the absence of target DNA provide insight into DNA-binding mechanisms of LuxR-type receptors.BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,520(2),399-405. |
| MLA | Wu, H,et al."Large conformation shifts of Vibrio cholerae VqmA dimer in the absence of target DNA provide insight into DNA-binding mechanisms of LuxR-type receptors".BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 520.2(2019):399-405. |
入库方式： OAI收割
来源：上海应用物理研究所
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