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Eric Martz
The first new influenza virus to emerge as an imminent pandemic threat in the 21st century is H1N1 swine flu. The drug oseltamivir (Tamiflu®) inhibits flu neuraminidase, a component necessary for virus spread, in susceptible flu strains. The development of oseltamivir was guided, in part, by crystallographically determined structures of flu neuraminidase, which is a homotetramer, shown with oseltamivir bound. Oseltamivir was designed to fit N2/N9 (neuraminidases from other strains of flu). Serendipitously, it also fits N1 by induced fit.

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H Matsunami, YH Yoon, VA Meshcheryakov, K Namba, FA Samatey. Scientific Reports 2016 doi: 10.1038/srep27399
A periplasmic flagellar chaperone protein, FlgA, is required for P-ring assembly in bacterial flagella of taxa such as Salmonella enterica or Escherichia coli. Here we present the open and closed crystal structures of FlgA from Salmonella enterica serovar Typhimurium, grown under different crystallization conditions. An intramolecular disulfide cross-linked form of FlgA caused a dominant negative effect on motility of the wild-type strain.

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Touching stretches cell membranes, opening mechanosensitive ion channels, leading to sensation by the nervous system. Pictured is the transmembrane region of a similar channel in bacteria. When closed, the narrow opening is lined by hydrophobic amino acid sidechains, making it non-conductive to ions.

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