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@article{1322749,
author = {Kubáň, Vojtěch and Nováček, Jiří and Bumba, Ladislav and Žídek, Lukáš},
article_location = {Dordrecht (Netherlands)},
article_number = {2},
doi = {http://dx.doi.org/10.1007/s12104-015-9625-z},
keywords = {FrpC; Self-processing module; Neisseria meningitidis; Intrinsically disordered proteins; Sparse sampling; Resolution-enhanced spectroscopy; Resonance assignment},
language = {eng},
issn = {1874-2718},
journal = {Biomolecular NMR Assignments},
title = {NMR assignment of intrinsically disordered self-processing module of the FrpC protein of Neisseria meningitidis},
url = {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},
volume = {9},
year = {2015}
}
TY - JOUR
ID - 1322749
AU - Kubáň, Vojtěch - Nováček, Jiří - Bumba, Ladislav - Žídek, Lukáš
PY - 2015
TI - NMR assignment of intrinsically disordered self-processing module of the FrpC protein of Neisseria meningitidis
JF - Biomolecular NMR Assignments
VL - 9
IS - 2
SP - 435-440
EP - 435-440
PB - Springer Netherlands
SN - 18742718
KW - FrpC
KW - Self-processing module
KW - Neisseria meningitidis
KW - Intrinsically disordered proteins
KW - Sparse sampling
KW - Resolution-enhanced spectroscopy
KW - Resonance assignment
UR - 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
L2 - 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
N2 - 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.
ER -
KUBÁŇ, Vojtěch, Jiří NOVÁČEK, Ladislav BUMBA and Lukáš ŽÍDEK. NMR assignment of intrinsically disordered self-processing module of the FrpC protein of Neisseria meningitidis. \textit{Biomolecular NMR Assignments}. Dordrecht (Netherlands): Springer Netherlands, 2015, vol.~9, No~2, p.~435-440. ISSN~1874-2718. Available from: https://dx.doi.org/10.1007/s12104-015-9625-z.
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