Prof. Mary Luckey's Home Page

Mary Luckey's Home Page

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Short Bio

maltoporinMy Ph.D. research showed that the TonA protein (now called FhuA) was the receptor for ferrichrome, which was the first identification of an iron transport protein in the bacterial outer membrane.  My postdoctoral work demonstrated the specificity of the purified LamB protein (maltoporin from E. coli) for uptake of maltose and maltodextrins in reconstituted liposomes.  My research group continued to focus on maltoporin structure and biogenesis, demonstrating that its two cysteines make an intrasubunit disulfide bond (later confirmed by the x-ray structure) that contributes to the thermostability of the trimer.  Our studies of the folding and assembly of the LamB trimer indicated the disulfide bond holds Loop 1 in the cavity and identified specific salt bridges involved in subunit interactions.  For twenty-eight years I taught courses in biochemistry, membrane biochemistry and cancer at SFSU.  I am author of the book, Membrane Structural Biology published by Cambridge University Press, now in its second edition.  I have three children and two grandchildren.
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