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NMR resonance assignments for the GSPII-C domain of the PilF ATPase from Thermus thermophilus in complex with c-di-GMP.

Biomol NMR Assign. 2019; 
KellerHeiko,KruseKerstin,AverhoffBeate,Duchardt-FernerElke,Wöhnert
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Bacterial Expression System … A DNA construct encoding a truncated version of PilF cor- responding to the isolated GSPII-C domain (amino acids 294–482) from T. thermophilus HB27 was commercially synthesized by GenScript (New Jersey, USA). The codon usage was optimized for expression in E. coli … Get A Quote

摘要

The natural transformation system of the thermophilic bacterium Thermus thermophilus is one of the most efficient DNA transport systems in terms of DNA uptake rate and promiscuity. The DNA transporter of T. thermophilus plays an important role in interdomain DNA transfer in hot environments. PilF is the traffic ATPase that provides the energy for the assembly of the DNA translocation machinery and the functionally linked type IV pilus system in T. thermophilus. In contrast to other known traffic ATPases, the N-terminal region of PilF harbors three consecutive domains with homology to general secretory pathway II (GSPII) domains. These GSPII-like domains influence pilus assembly, twitching motility and trans... More

关键词

ATPase,NMR-assignments,PilF,Triple resonance experiments,c-di