title: NMR assignment of intrinsically disordered self-processing module of the FrpC protein of Neisseria meningitidis.
abstract: The self-processing module (SPM) is an internal segment of the FrpC protein (P415-F591) secreted by the pathogenic Gram-negative bacterium Neisseria meningitidis during meningococcal infection of human upper respiratory tract. SPM mediates 'protein trans-splicing', a unique natural mechanism for editing of proteins, which involves a calcium-dependent autocatalytic cleavage of the peptide bond between D414 and P415 and covalent linkage of the cleaved fragment through its carboxy-terminal group of D414 to [Formula: see text]-amino group of lysine residue within a neighboring polypeptide chain. We present an NMR resonance assignment of the calcium-free SPM, which displays characteristic features of intrinsically disordered proteins. Non-uniformly sampled 5D HN(CA)CONH, 4D HCBCACON, and HCBCANCO spectra were recorded to resolve poorly dispersed resonance frequencies of the disordered protein and 91 % of SPM residues were unambiguously assigned. Analysis of the chemical shifts revealed that two regions of the intrinsically disordered SPM (A95-S101 and R120-I127) have a tendency to form a helical structure, whereas the residues P1-D7 and G36-A40 have the propensity to adopt a [Formula: see text]-structure.
authors.affiliation: CEITEC, Masaryk University, Kamenice 5, 62500, Brno, Czech Republic.
authors.forename: Vojtěch
authors.initials: V
authors.lastname: Kubáň
authors.affiliation: CEITEC, Masaryk University, Kamenice 5, 62500, Brno, Czech Republic.
authors.forename: Jiří
authors.initials: J
authors.lastname: Nováček
authors.affiliation: Institute of Microbiology of the ASCR, v. v. i, Vídeňská 1083, 14220, Prague 4, Czech Republic.
authors.forename: Ladislav
authors.initials: L
authors.lastname: Bumba
authors.affiliation: CEITEC, Masaryk University, Kamenice 5, 62500, Brno, Czech Republic. lzidek@chemi.muni.cz.
authors.forename: Lukáš
authors.initials: L
authors.lastname: Žídek
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D064267:Intrinsically Disordered Proteins / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry*; D009345:Neisseria meningitidis / Q000378:metabolism*; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary
chemical_list: D001426:Bacterial Proteins; D064267:Intrinsically Disordered Proteins; D008565:Membrane Proteins; C083530:frpC protein, Neisseria meningitidis
keywords: FrpC; Intrinsically disordered proteins; Neisseria meningitidis; Resolution-enhanced spectroscopy; Resonance assignment; Self-processing module; Sparse sampling