Point mutations in two conserved glycine residues within the integral membrane protein FhuB affect iron(III) hydroxamate transport.

doi:10.1007/BF00266243

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Point mutations in two conserved glycine residues within the integral membrane protein FhuB affect iron(III) hydroxamate transport.

Molecular & general genetics : MGG - 1 Apr 1992

Köster W, Böhm B

Abstract excerpt

A region of substantial homology, comprising 32 amino acids around a highly conserved glycine residue, is located near the C-terminal ends of the hydrophobic Fhu, Fec, Fep, Fat, and Btu transport proteins involved in the uptake of ferrisiderophores and vitamin B12 into Escherichia coli and Vibrio anguillarum. Furthermore, a region similar in location and sequence containing an invariant glycine at an equivalent...

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Point mutations in two conserved glycine residues within the integral membrane protein FhuB affect iron(III) hydroxamate transport.

Abstract excerpt

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Point mutations in two conserved glycine residues within the integral membrane protein FhuB affect iron(III) hydroxamate transport.

Abstract excerpt

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