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

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[NMR paper] NMR assignment of intrinsically disordered self-processing module of the FrpC protein of Neisseria meningitidis.

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07-05-2015, 02:07 AM

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

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

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

Biomol NMR Assign. 2015 Jul 3;

Authors: Kubá? V, Nová?ek J, Bumba L, Žídek L

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.

PMID: 26138689 [PubMed - as supplied by publisher]

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