title: Structural basis of the interaction between the putative adhesion-involved and iron-regulated FrpD and FrpC proteins of Neisseria meningitidis.
abstract: 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-Pro415peptide 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 FrpC1-414binding, which enabled localization of FrpD within the low-resolution SAXS model of the FrpD-FrpC1-414complex. Moreover, the trans-splicing activity of FrpC resulted in covalent linkage of the FrpC1-414fragment to plasma membrane proteins of epithelial cells in vitro, suggesting that formation of the FrpD-FrpC1-414complex may be involved in the interaction of meningococci with the host cell surface.
authors.affiliation: Faculty of Science, University of South Bohemia Ceske Budejovice, Branisovska 1760, 37005 Ceske Budejovice, Czech Republic.|Center for Nanobiology and Structural Biology, Institute of Microbiology, Czech Academy of Sciences, Zamek 136, 37333 Nove Hrady, Czech Republic.
authors.forename: Ekaterina
authors.initials: E
authors.lastname: Sviridova
authors.affiliation: Institute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Flemingovo nam. 2, 16610 Prague, Czech Republic.
authors.forename: Pavlina
authors.initials: P
authors.lastname: Rezacova
authors.affiliation: Center for Nanobiology and Structural Biology, Institute of Microbiology, Czech Academy of Sciences, Zamek 136, 37333 Nove Hrady, Czech Republic.|Institute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Flemingovo nam. 2, 16610 Prague, Czech Republic.
authors.forename: Alexey
authors.initials: A
authors.lastname: Bondar
authors.affiliation: Institute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Flemingovo nam. 2, 16610 Prague, Czech Republic.
authors.forename: Vaclav
authors.initials: V
authors.lastname: Veverka
authors.affiliation: Institute of Microbiology, Czech Academy of Sciences, Videnska 1083, 14220 Prague, Czech Republic.
authors.forename: Petr
authors.initials: P
authors.lastname: Novak
authors.affiliation: EMBL Hamburg Outstation, c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany.
authors.forename: Gundolf
authors.initials: G
authors.lastname: Schenk
authors.affiliation: EMBL Hamburg Outstation, c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany.
authors.forename: Dmitri I
authors.initials: DI
authors.lastname: Svergun
authors.affiliation: Faculty of Science, University of South Bohemia Ceske Budejovice, Branisovska 1760, 37005 Ceske Budejovice, Czech Republic.|Center for Nanobiology and Structural Biology, Institute of Microbiology, Czech Academy of Sciences, Zamek 136, 37333 Nove Hrady, Czech Republic.
authors.forename: Ivana
authors.initials: I
authors.lastname: Kuta Smatanova
authors.affiliation: Institute of Microbiology, Czech Academy of Sciences, Videnska 1083, 14220 Prague, Czech Republic.
authors.forename: Ladislav
authors.initials: L
authors.lastname: Bumba
mesh_terms: D000595:Amino Acid Sequence / Q000235:genetics; D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D002448:Cell Adhesion / Q000235:genetics; D006801:Humans; D007501:Iron / Q000737:chemistry / Q000378:metabolism; D033862:Iron-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D008074:Lipoproteins / Q000737:chemistry / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics; D009345:Neisseria meningitidis / Q000737:chemistry* / Q000235:genetics; D033902:Periplasmic Binding Proteins / Q000737:chemistry / Q000378:metabolism; D014961:X-Ray Diffraction
chemical_list: D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D033862:Iron-Binding Proteins; D008074:Lipoproteins; D008565:Membrane Proteins; D033902:Periplasmic Binding Proteins; C083530:frpC protein, Neisseria meningitidis; D007501:Iron