Investigating the roles of the conserved Cu²⁺-binding residues on Brucella FtrA in producing conformational stability and functionality.

ABSTRACT: Brucella is a zoonotic pathogen requiring iron for its survival and acquires this metal through the expression of several high-affinity uptake systems. Of these, the newly discovered ferrous iron transporter, FtrABCD, is proposed to take part in ferrous iron uptake. Sequence homology shows that, FtrA, the proposed periplasmic ferrous-binding component, is a P19-type protein (a periplasmic protein from C. jejuni which shows Cu²⁺ dependent iron affinity). Previous structural and biochemical studies on other P19 systems have established a Cu²⁺ dependent Mn²⁺ affinity as well as formation of homodimers for these systems. The Cu²⁺ coordinating amino acids from these proteins are conserved in Brucella FtrA, hinting towards similar properties. However,

SUBMITTER: Banerjee S 

PROVIDER: S-EPMC7484176 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature