Backbone resonance assignments of the outer membrane lipoprotein FrpD from Neisseria meningitidis
Language English Country Netherlands Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Lipoproteins chemistry MeSH
- Neisseria meningitidis metabolism MeSH
- Nuclear Magnetic Resonance, Biomolecular * MeSH
- Bacterial Outer Membrane Proteins chemistry MeSH
- Amino Acid Sequence MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Lipoproteins MeSH
- Bacterial Outer Membrane Proteins 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.
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