This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The novel crystallographic structure solution of bacterial membrane proteins is being undertaken in this proposal. We have crystallized several components of the type III secretion apparatus which spans the inner and outer membrane of pathogenic bacteria, and allows for the passage of bacterial virulence proteins into the host cell. This secretion apparatus is highly conserved amongst several gram negative pathogens including Salmonella, Enterhemmorhaghic E. coli, Psedomonas, Bordatella and Shigella. Seleno-methionine phasing of EscN (an essential ATPase of the secretion apparatus at the bacterial inner membrane), a complex of EscJ and EscC (which are presumed to form a large ring like structure in the bacterial outer membrane), and EspB (presumed to form the pore in the human host membrane) will be pursued. Additionally, the phasing of a key virulence factor that is translocated into the host cell, then inserted into host cell membranes to facilitate bacterial adhesion (TIR for translocated intimin receptor) will also be pursued.
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