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NMR assignment of intrinsically disordered self-processing module of the FrpC protein of Neisseria meningitidis
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SYSNO ASEP 0452973 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title NMR assignment of intrinsically disordered self-processing module of the FrpC protein of Neisseria meningitidis Author(s) Kubáň, V. (CZ)
Nováček, J. (CZ)
Bumba, Ladislav (MBU-M) RID, ORCID
Žídek, L. (CZ)Source Title Biomolecular NMR Assignments. - : Springer - ISSN 1874-2718
Roč. 9, č. 2 (2015), s. 435-440Number of pages 6 s. Language eng - English Country DE - Germany Keywords FrpC ; Self-processing module ; Neisseria meningitidis Subject RIV EE - Microbiology, Virology R&D Projects GAP207/11/0717 GA ČR - Czech Science Foundation (CSF) Institutional support MBU-M - RVO:61388971 UT WOS 000361440100046 DOI 10.1007/s12104-015-9625-z Annotation 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 -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. Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2016
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