title: Backbone resonance assignments of the outer membrane lipoprotein FrpD from Neisseria meningitidis.
abstract: 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.
authors.affiliation: Institute of Microbiology of the ASCR, v.v.i., Videnska 1083, Prague, 142 20, Czech Republic.
authors.forename: Ladislav
authors.initials: L
authors.lastname: Bumba
authors.forename: Ekaterina
authors.initials: E
authors.lastname: Sviridova
authors.forename: Ivana
authors.initials: I
authors.lastname: Kutá Smatanová
authors.forename: Pavlína
authors.initials: P
authors.lastname: Řezáčová
authors.forename: Václav
authors.initials: V
authors.lastname: Veverka
mesh_terms: D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D008074:Lipoproteins / Q000737:chemistry*; D009345:Neisseria meningitidis / Q000378:metabolism*; D019906:Nuclear Magnetic Resonance, Biomolecular
chemical_list: D001425:Bacterial Outer Membrane Proteins; D008074:Lipoproteins