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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Andrea Gorrell, Leni Rose, William Eisbrenner, David Canner, Michal Harel, Alexander Berchansky