Residual Helicity at the Active Site of the Histidine Phosphocarrier, HPr, Modulates Binding Affinity to Its Natural Partners.

ABSTRACT: The phosphoenolpyruvate-dependent phosphotransferase system (PTS) modulates the preferential use of sugars in bacteria. The first proteins in the cascade are common to all organisms (EI and HPr). The active site of HPr involves a histidine (His15) located immediately before the beginning of the first α-helix. The regulator of sigma D (Rsd) protein also binds to HPr. The region of HPr comprising residues Gly9-Ala30 (HPr^9-30), involving the first α-helix (Ala16-Thr27) and the preceding active site loop, binds to both the N-terminal region of EI and intact Rsd. HPr^9-30 is mainly disordered. We attempted to improve the affinity of HPr^9-30 to both proteins by mutating its sequence to increase its helicity. We designed peptides that led to a marginally larger pop

SUBMITTER: Neira JL 

PROVIDER: S-EPMC8509676 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature