NMR Solution Structure of the N-Terminal GSPII Domain from the Thermus Thermophilus Traffic ATPase PilF and Reconstruction of its c-di-GMP Binding Capability.

ABSTRACT: The cyclic dinucleotide c-di-GMP is an important second messenger molecule in bacteria and interacts with a variety of receptor molecules including RNA and protein domains. An important class of c-di-GMP-binding protein domains are the general secretory pathway type II (GSPII) domains as exemplified by the N-terminal domain of the ATPase MshE from Vibrio cholerae (MshEN). MshEN binds monomeric c-di-GMP via two consecutive copies of a 24-residue sequence motif, which form a compact 4-α-helical bundle. The ATPase PilF from Thermus thermophilus regulates pilus formation, motility and DNA-uptake. Its N-terminal section contains three consecutive GSPII domains (GSPII-A-GSPII-C) all with considerable sequence homology to MshEN. While the GSPII-B and the GSPII-C domains bind c-di-GMP, the GSPII-A

SUBMITTER: Neißner K 

PROVIDER: S-EPMC12002112 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature