NMR assignment of intrinsically disordered self-processing module of the FrpC protein of Neisseria meningitidis
| Authors | |
|---|---|
| Year of publication | 2015 |
| Type | Article in Periodical |
| Magazine / Source | Biomolecular NMR Assignments |
| MU Faculty or unit | |
| Citation | |
| Web | http://download.springer.com/static/pdf/605/art%253A10.1007%252Fs12104-015-9625-z.pdf?originUrl=http%3A%2F%2Flink.springer.com%2Farticle%2F10.1007%2Fs12104-015-9625-z&token2=exp=1451977460~acl=%2Fstatic%2Fpdf%2F605%2Fart%25253A10.1007%25252Fs12104-015-96 |
| Doi | http://dx.doi.org/10.1007/s12104-015-9625-z |
| Field | Microbiology, virology |
| Keywords | FrpC; Self-processing module; Neisseria meningitidis; Intrinsically disordered proteins; Sparse sampling; Resolution-enhanced spectroscopy; Resonance assignment |
| Description | 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. |
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