FhuD: Difference between revisions
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==OVERVIEW== | ==OVERVIEW== | ||
Siderophore-binding proteins can be found in both Gram-positive and Gram-negative bacteria in divisions: hydroxamates, catecholates, and carboxylates. In Escherichia coli. (E. coli) the ATP-binding cassette- type (ABC-type) protein FhuD is a common periplasmic protein which facilitates the transport of a variety of hydoxamate siderophores to the inner membrane-associated proteins FhuB and FhuC. The structure of FhuD is atypical for periplasmic ligand binding protein due to its bilobal mixture of two α/β domains connected by long α-helix. | Siderophore-binding proteins can be found in both Gram-positive and Gram-negative bacteria in divisions: hydroxamates, catecholates, and carboxylates. In Escherichia coli. (E. coli) the ATP-binding cassette- type (ABC-type) protein FhuD (part of the “helical backbone” metal receptor superfamily) is a common periplasmic protein which facilitates the transport of a variety of hydoxamate siderophores to the inner membrane-associated proteins FhuB and FhuC. The structure of FhuD is atypical for periplasmic ligand binding protein due to its bilobal mixture of two α/β domains connected by long α-helix. | ||
==PROTEIN STRUCTURE== | ==PROTEIN STRUCTURE== | ||
