期刊
STRUCTURE
卷 19, 期 4, 页码 577-587出版社
CELL PRESS
DOI: 10.1016/j.str.2011.01.012
关键词
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资金
- Deutsche Forschungsgemeinschaft [BE 1911/4-3]
- Center for Biomolecular Magnetic Resonance (BMRZ)
- Cluster of Excellence Frankfurt (Macromolecular Complexes)
- Volkswagen Foundation
The Rcs-signaling system is one of the most remarkable phosphorelay pathways in Enterobacteriaceae, comprising several membrane-bound and soluble proteins. Within the complex phosphotransfer pathway, the histidine phosphotransferase (HPt) domain of the RcsD membrane-bound component serves as a crucial factor in rnodulating the phosphorylation state of the transcription factor RcsB. We have identified a new domain, RcsD-ABL, located N terminally to RcsD-HPt that interacts with RcsB as well. We have determined its structure, characterized its interaction interface with RcsB, and built a structural model of the complex of the RcsD-ABL domain with RcsB. Our results indicate that the effector domain of RcsB, which normally binds to DNA, is recognized by RcsD-ABL, whereas the HPt domain interacts with the phosphoreceiver domain of RcsB.
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