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Abstract:
Small protein B (SmpB) is an essential molecule in trans-translation which is a universal biological pathway for protein synthesis in bacteria. Trans-translation can release stalled ribosomes from defective mRNAs and target tag-protein fragments for degradation, and then restart protein synthesis. The SmpB-tmRNA complex coordinating with other components of the trans-translation system, plays vital roles in Mycobacterium tuberculosis under both stress conditions and non-replicating conditions. Thus, elucidation of molecular details and dynamic properties of the SmpB-tmRNA interaction is a crucial step towards effectively blocking trans-translation process to shorten the duration of tuberculosis treatment. Here, we report resonance assignments for 1H, 13C and 15N of M. tuberculosis SmpB (MtSmpB, spanning residues 4–133) protein determined by a suite of 2D/3D heteronuclear NMR experiments along with predicted the secondary structure. © 2017, Springer Science+Business Media Dordrecht.
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Biomolecular NMR Assignments
ISSN: 1874-2718
Year: 2017
Issue: 2
Volume: 11
Page: 175-179
0 . 5 9 3
JCR@2017
0 . 8 0 0
JCR@2023
ESI HC Threshold:231
JCR Journal Grade:4
CAS Journal Grade:4
Cited Count:
WoS CC Cited Count: 0
SCOPUS Cited Count: 1
ESI Highly Cited Papers on the List: 0 Unfold All
WanFang Cited Count:
Chinese Cited Count:
30 Days PV: 1
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