Conjuring up a ghost: structural and functional characterization of FhuF, a ferric siderophore reductase from E. coli.

ABSTRACT: Iron is a fundamental element for virtually all forms of life. Despite its abundance, its bioavailability is limited, and thus, microbes developed siderophores, small molecules, which are synthesized inside the cell and then released outside for iron scavenging. Once inside the cell, iron removal does not occur spontaneously, instead this process is mediated by siderophore-interacting proteins (SIP) and/or by ferric-siderophore reductases (FSR). In the past two decades, representatives of the SIP subfamily have been structurally and biochemically characterized; however, the same was not achieved for the FSR subfamily. Here, we initiate the structural and functional characterization of FhuF, the first and only FSR ever isolated. FhuF is a globular monomeric protein mainly composed by α-heli

SUBMITTER: Trindade IB 

PROVIDER: S-EPMC8068687 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature