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 two divisions: hydroxamates and catecholates. 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. FhuD is part of the superfamily "helical backbone" metal receptors and the family of periplasmic ferric siderophore binding protein FhuD. 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 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==