The structural basis for high-affinity c-di-GMP binding to the GSPII-B domain of the traffic ATPase PilF from Thermus thermophilus.

c-di-GMP is an important second messenger in bacteria regulating, for example motility, biofilm formation, cell wall biosynthesis, infectivity, and natural transformability. It binds to a multitude of intracellular receptors. This includes proteins containing general secretory pathway II (GSPII) domains such as the N-terminal domain of the Vibrio cholerae ATPase MshE (MshEN) which binds c-di-GMP with two copies of a 24-amino acids sequence motif.

H, C, and N backbone chemical-shift assignments of SARS-CoV-2 non-structural protein 1 (leader protein).

The current COVID-19 pandemic caused by the Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) has become a worldwide health crisis, necessitating coordinated scientific research and urgent identification of new drug targets for treatment of COVID-19 lung disease. The covid19-nmr consortium seeks to support drug development by providing publicly accessible NMR data on the viral RNA elements and proteins. The SARS-CoV-2 genome comprises a single RNA of about 30 kb in length, in which 14 open reading frames (ORFs) have been annotated, and encodes approximately 30 proteins.

NMR resonance assignments for the GSPII-B domain of the traffic ATPase PilF from Thermus thermophilus in the apo and the c-di-GMP-bound state.

The PilF protein from the thermophilic bacterium Thermus thermophilus is a traffic ATPase powering the assembly of the DNA translocation machinery as well as of type 4 pili. Thereby PilF mediates the natural transformability of T. thermophilus.