IDENTIFYING THE METAL SITE ENVIRONMENTS IN P19 WITH EXAFS

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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. P19 is a small (17500 Da) periplasmic protein isolated from the bacterium Campylobacter jejuni, a common food borne human pathogen. In C. jejuni, P19 expression is both iron and oxygen regulated (Palyada et al 2004). ChpA (copper handling protein) is a P19 orthologue characterized in a strain of magnetotactic bacteria. These unusual bacteria contain an intracellular magnetosome formed from magnets aligned as an arrow (Blakemore, 1975; Bazylinski & Frankel, 2004). This magnetosome is thought to sense the earth magnetic field enabling the bacteria to swim to the microaerobic layer of the water pool (pond, reservoir). Disruption of the gene for ChpA has shown that this protein is required for magnetosome production (Dubbels et al, 2004). ChpA as isolated from magnetotatic bacteria was shown to be a homodimer that binds copper. Inspection of the genomic context of both ChpA and P19 suggests that these orthologues are likely involved in iron uptake.