U.S. Department of Health and Human Services

Laboratory of Molecular Biology

Susan K. Buchanan, Ph.D., Chief

​Research Images

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Introduction to the Hermes transposon #1This image depicts some of the reasons why we study Hermes transposition.Enlarge
Introduction to the Hermes transposon #2This image depicts a schematic representation of the cut-and-paste reaction catalyzed by the Hermes transposase. For simplicity, the reactions are shown for only one end (the so-called Left End) of the transposon, so you must imagine the identical reactions are carried out on the Right End (not shown). For comparison, the reaction pathway for a simple bacterial transposase (carried by the Tn5 transposon) is also shown.Enlarge
The domain organization of the Hermes transposase and the 3D structure of the protein aloneThe Hermes transposase consists of 612 amino acids. On the monomer level, it is a multidomain protein (domains are represented as colored boxes in the schematic on top) organized around a central catalytic core (orange) that is structurally related to E. coli RNase H.Enlarge
Neisserial Iron Import ComplexNeisseria survive in the human host by utilizing surface receptors to pirate iron from human iron binding proteins. Based on our studies, we were able to describe what the Neisserial import complex looks like at the surface of the pathogen. Shown here is the iron transporter TbpA (purple, red glow indicates iron passage), the co-receptor TbpB (purple, top), the human iron binding protein transferrin (orange), periplasmic proteins FbpA (dark green), and TonB (light green).Enlarge
Structure of the TLR3-ECDThis image depicts the structure of the TLR3-ECD. The TLR3-ECD consists of 23 LRRs that form a horseshoe-like solenoid with two capping motifs. The molecule has a surprisingly flat profile. There are 11 visible glycosylation sites. Figure 1 BBA, 2009.Enlarge