Structural insight into the novel iron-coordination and domain interactions of transferrin-1 from a model insect, Manduca sexta.

ABSTRACT: Transferrins function in iron sequestration and iron transport by binding iron tightly and reversibly. Vertebrate transferrins coordinate iron through interactions with two tyrosines, an aspartate, a histidine, and a carbonate anion, and conformational changes that occur upon iron binding and release have been described. Much less is known about the structure and functions of insect transferrin-1 (Tsf1), which is present in hemolymph and influences iron homeostasis mostly by unknown mechanisms. Amino acid sequence and biochemical analyses have suggested that iron coordination by Tsf1 differs from that of the vertebrate transferrins. Here we report the first crystal structure (2.05 Å resolution) of an insect transferrin. Manduca sexta (MsTsf1) in the holo form exhibits a bilobal fold simila

SUBMITTER: Weber JJ 

PROVIDER: S-EPMC7784759 | biostudies-literature | 2021 Feb

REPOSITORIES: biostudies-literature