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© Research
Publication : Biomolecular NMR assignments

H, N and C resonance assignments and secondary structure of PulG, the major pseudopilin from Klebsiella oxytoca type 2 secretion system

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Biomolecular NMR assignments - 03 Mar 2017

López-Castilla A, Vitorge B, Khoury L, Morellet N, Francetic O, Izadi-Pruneyre N

Link to Pubmed [PMID] – 28258547

Biomol NMR Assign 2017 Oct;11(2):155-158

Bacteria use complex transporters to secrete functionally relevant proteins to the extracellular medium. The type 2 secretion system (T2SS) translocates folded proteins involved in bacterial nutrient acquisition, virulence and adaptation. The T2SS pseudopilus is a periplasmic filament, assembled by the polymerization of PulG subunits, the major pseudopilin. Pseudopilin proteins have a conserved N-terminal hydrophobic segment followed by a more variable C-terminal periplasmic and globular domain. To better understand the mechanism of assembly and function of the T2SS, we have been studying the structure and dynamics of PulG by NMR, as well as its interaction with other components of the secretion machinery. As a first step on this study, here we reported the chemical shift assignments of PulG C-terminal domain and its secondary structure prediction based on NMR data.

https://www.ncbi.nlm.nih.gov/pubmed/28258547