期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 384, 期 2, 页码 422-435出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2008.09.017
关键词
bacterial signal transduction; cyclophilin; histidine kinase inhibition; small-angle scattering; neutron contrast variation
资金
- Australian Research Council Federation Fellowship
- U.S. Department of Energy [DE-FG02-05ER64026]
- National Health and Medical Research Council [352434]
- Australian Institute of Nuclear Science and Engineering Postgraduate Research Award
- National Institute of Standards and Technology (NIST)
- U.S. Department of Commerce
- National Science Foundation under Agreement [DMR-0454672]
- Access to Major Research Facilities Programme [06/07-N-13]
- Australian Proteome Analysis Facility
- Australian Government's Major National Facilities program
The sensor histidine kinase A (KinA) from Bacillus subtilis triggers a phosphorelay that activates sporulation. The antikinase KipI prevents sporulation by binding KinA and inhibiting the autophosphorylation reaction. Using neutron contrast variation, mutagenesis, and fluorescence data, we show that two KipI monomers bind via their C-domains at a conserved proline in the KinA dimerization and histidine-phosphotransfer (DHp) domain. Our crystal structure of the KipI C-domain reveals the binding motif has a distinctive hydrophobic groove formed by a five-stranded antiparallel beta-sheet; a characteristic of the cyclophilin family of proteins that bind prolines and often act as cis-trans peptidyl-prolyl isomerases. We propose that the DHp domain of KinA transmits conformational signals to regulate kinase activity via this proline-mediated interaction. Given that both KinA and KipI homologues are widespread in the bacterial kingdom, this mechanism has broad significance in bacterial signal transduction. (C) 2008 Elsevier Ltd. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据