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.<ref name="lu">PMID: 11805094</ref> 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.<ref name="lu"/> 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.<ref name="lu"/>,<ref name="la">PMID: 10742172</ref> | Siderophore-binding proteins can be found in both Gram-positive and Gram-negative bacteria in divisions: hydroxamates, catecholates, and carboxylates.<ref name="lu">PMID: 11805094</ref> 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.<ref name="lu"/> 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.<ref name="lu"/>,<ref name="la">PMID: 10742172</ref> | ||
==PROTEIN STRUCTURE== | ==PROTEIN STRUCTURE== | ||
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==3D structures of FhuD== | ==3D structures of FhuD== | ||
[[Ferric hydroxamate uptake receptor]]. | |||
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==REFERENCES== | ==REFERENCES== | ||