Fe(II), Mn(II), and Zn(II) Binding to the C-Terminal Region of FeoB Protein: An Insight into the Coordination Chemistry and Specificity of the Escherichia coli Fe(II) Transporter.

ABSTRACT: The interactions between two peptide ligands [Ac₇₆₃CCAASTTGDCH₇₇₃ (P1) and Ac₇₄₃RRARSRVDIELLATRKSVSSCCAASTTGDCH₇₇₃ (P2)] derived from the cytoplasmic C-terminal region of Eschericha coli FeoB protein and Fe(II), Mn(II), and Zn(II) ions were investigated. The Feo system is regarded as the most important bacterial Fe(II) acquisition system, being one of the key virulence factors, especially in anaerobic conditions. Located in the inner membrane of Gram-negative bacteria, FeoB protein transports Fe(II) from the periplasm to the cytoplasm. Despite its crucial role in bacterial pathogenicity, the mechanism in which the metal ion is trafficked through the membrane is not yet elucidated. In the gammaproteobacteria class, the cytopla

SUBMITTER: Orzel B 

PROVIDER: S-EPMC10647171 | biostudies-literature | 2023 Nov

REPOSITORIES: biostudies-literature