Počet záznamů: 1  

NMR assignment of intrinsically disordered self-processing module of the FrpC protein of Neisseria meningitidis

  1. 1.
    SYSNO ASEP0452973
    Druh ASEPJ - Článek v odborném periodiku
    Zařazení RIVJ - Článek v odborném periodiku
    Poddruh JČlánek ve WOS
    NázevNMR assignment of intrinsically disordered self-processing module of the FrpC protein of Neisseria meningitidis
    Tvůrce(i) Kubáň, V. (CZ)
    Nováček, J. (CZ)
    Bumba, Ladislav (MBU-M) RID, ORCID
    Žídek, L. (CZ)
    Zdroj.dok.Biomolecular NMR Assignments. - : Springer - ISSN 1874-2718
    Roč. 9, č. 2 (2015), s. 435-440
    Poč.str.6 s.
    Jazyk dok.eng - angličtina
    Země vyd.DE - Německo
    Klíč. slovaFrpC ; Self-processing module ; Neisseria meningitidis
    Vědní obor RIVEE - Mikrobiologie, virologie
    CEPGAP207/11/0717 GA ČR - Grantová agentura ČR
    Institucionální podporaMBU-M - RVO:61388971
    UT WOS000361440100046
    DOI10.1007/s12104-015-9625-z
    AnotaceThe 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 -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 beta-structure.
    PracovištěMikrobiologický ústav
    KontaktEliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231
    Rok sběru2016
Počet záznamů: 1  

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