15525636 OR The Neisseria meningitidis outer membrane lipoprotein FrpD binds the RTX protein FrpC Dotaz Zobrazit nápovědu
- MeSH
- bakteriální proteiny genetika metabolismus MeSH
- lipoproteiny genetika metabolismus MeSH
- membránové proteiny genetika chemie metabolismus MeSH
- Neisseria meningitidis genetika MeSH
- proteiny vnější bakteriální membrány genetika metabolismus MeSH
- techniky in vitro MeSH
- vápník farmakologie MeSH
- železo metabolismus MeSH
The iron-regulated FrpD protein is a unique lipoprotein embedded into the outer membrane of the Gram-negative bacterium Neisseria meningitidis. The biological function of FrpD remains unknown but might consist in anchoring to the bacterial cell surface the Type I-secreted FrpC protein, which belongs to a Repeat in ToXins (RTX) protein family and binds FrpD with very high affinity (K(d) = 0.2 nM). Here, we report the backbone (1)H, (13)C, and (15)N chemical shift assignments for the FrpD(43-271) protein that allow us to characterize the intimate interaction between FrpD and the N-terminal domain of FrpC.
The iron-regulated protein FrpD from Neisseria meningitidis is an outer membrane lipoprotein that interacts with very high affinity (Kd ~ 0.2 nM) with the N-terminal domain of FrpC, a Type I-secreted protein from the Repeat in ToXin (RTX) protein family. In the presence of Ca2+, FrpC undergoes Ca2+ -dependent protein trans-splicing that includes an autocatalytic cleavage of the Asp414-Pro415 peptide bond and formation of an Asp414-Lys isopeptide bond. Here, we report the high-resolution structure of FrpD and describe the structure-function relationships underlying the interaction between FrpD and FrpC1-414. We identified FrpD residues involved in FrpC1-414 binding, which enabled localization of FrpD within the low-resolution SAXS model of the FrpD-FrpC1-414 complex. Moreover, the trans-splicing activity of FrpC resulted in covalent linkage of the FrpC1-414 fragment to plasma membrane proteins of epithelial cells in vitro, suggesting that formation of the FrpD-FrpC1-414 complex may be involved in the interaction of meningococci with the host cell surface.
- MeSH
- bakteriální proteiny chemie genetika MeSH
- buněčná adheze genetika MeSH
- difrakce rentgenového záření MeSH
- lidé MeSH
- lipoproteiny chemie metabolismus MeSH
- membránové proteiny chemie genetika MeSH
- Neisseria meningitidis chemie genetika MeSH
- periplazmatické vazebné proteiny chemie metabolismus MeSH
- proteiny vázající železo chemie metabolismus MeSH
- proteiny vnější bakteriální membrány metabolismus MeSH
- sekvence aminokyselin genetika MeSH
- železo chemie metabolismus MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
