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.

Download full-text PDF

Source
http://dx.doi.org/10.1007/s12104-012-9451-5DOI Listing

Publication Analysis

Top Keywords

outer membrane
8
neisseria meningitidis
8
frpd
5
backbone resonance
4
resonance assignments
4
assignments outer
4
membrane lipoprotein
4
lipoprotein frpd
4
frpd neisseria
4
meningitidis iron-regulated
4

Similar Publications

The outer membrane is the defining structure of Gram-negative bacteria. We previously demonstrated that it is a major load-bearing component of the cell envelope and is therefore critical to the mechanical robustness of the bacterial cell. Here, to determine the key molecules and moieties within the outer membrane that underlie its contribution to cell envelope mechanics, we measured cell-envelope stiffness across several sets of mutants with altered outer-membrane sugar content, protein content, and electric charge.

View Article and Find Full Text PDF

A historical perspective on the multifunctional outer membrane channel protein TolC in Escherichia coli.

NPJ Antimicrob Resist

January 2025

College of Biological Sciences, Department of Molecular and Cellular Biology, University of Guelph, 50 Stone Rd E, Guelph, ON, Canada.

Since its discovery nearly 60 years ago, TolC has been associated with various cellular functions in Escherichia coli, including the efflux of environmental stressors and virulence factors. It also acts as a receptor for specific bacteriophages and the colicin E1 toxin. This review highlights key discoveries over the past six decades and emphasizes the remaining gaps in understanding how TolC contributes to physiological functions in E.

View Article and Find Full Text PDF

Constitutive mitochondrial dynamics ensure quality control and metabolic fitness of cells, and their dysregulation has been implicated in various human diseases. The large GTPase Dynamin-related protein 1 (Drp1) is intimately involved in mediating constitutive mitochondrial fission and has been implicated in mitochondrial cell death pathways. During ferroptosis, a recently identified type of regulated necrosis driven by excessive lipid peroxidation, mitochondrial fragmentation has been observed.

View Article and Find Full Text PDF

The Acinetobacter baumannii is a member of the "ESKAPE" bacteria responsible for many serious multidrug-resistant (MDR) illnesses. This bacteria swiftly adapts to environmental cues leading to the emergence of multidrug-resistant variants, particularly in hospital/medical settings. In this work, we have demonstrated the outer membrane protein 33-36 (Omp33-36) porin as a potential therapeutic target in A.

View Article and Find Full Text PDF

: Since 2008, following clinical studies conducted on children that revealed the ability of the β-adrenergic antagonist propranolol to inhibit capillary growth in infantile hemangiomas (IHs), its oral administration has become the first-line treatment for IHs. Although oral propranolol therapy at a dosage of 3 mg/kg/die is effective, it can cause systemic adverse reactions. This therapy is not necessarily applicable to all patients.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!