1H, 15N, 13C resonnance assigments and secondary structure of PulL, a component of the Klebsiella oxytoca type II secretion system

1H, 15 N and 13C resonance assignments of the C-terminal domain of PulL, a component of the Klebsiella oxytoca type II secretion system.

chemical shift assignement, type II secretion system, PulL, Klebsiella oxytoca, secondary structure

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Type II secretion systems (T2SS) allow Gram-negative bacteria to transport toxins and enzymes from the periplasm to the external milieu.
This system is important for the pathogenicity of bacteria.
To drive secretion, T2SS assemble periplasmic filaments called pseudopili, closely related to bacterial type IV pili.
Pseudopilus assembly is orchestrated by the inner membrane subcomplex called the assembly platform, which is connected to the cytoplasmic ATPase motor.
In the Klebsiella oxytoca T2SS, the PulL protein from the assembly platform is essential for pseudopilus assembly and protein secretion.
To understand the molecular basis of PulL function, we used solution NMR to study its structure and interactions with other components of the machinery.
Here we report the chemical shift assignments of the C-terminal periplasmic domain of PulL and its secondary structure based on NMR data.

PulL 400uM, in Hepes 50mM pH6.5, NaCl, 50 mM