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Extra resources for Antibiotics
And another kinase FomA are related and (iv) initiation of X-ray crystallographic investigations of the structure of FosC. It is anticipated that this investigation will establish the mechanistic and structural foundation for design of new drugs to counter resistance to fosfomycin. The project is a response to program announcement PA-97-026, Aspergillosis, Ehrlichioses and Drug Resistance. ; Chief; None; Oregon Health & Science University Portland, or 972393098 Timing: Fiscal Year 2001; Project Start 01-SEP-1997; Project End 31-MAY-2006 Summary: Prematurity is the leading cause of neonatal morbidity and mortality in the United States.
A rapid temperature quench methodology will be developed to isolate the potential intermediate(s) for NMR structural studies. Multinuclear NMR analysis of the interaction of the synthases with various labeled substrate analogues will be utilized to observe abortive intermediates and substrate analogs designed to "stabilize" this potential abortive intermediate(s) will be used to further understand the mechanisms of these reactions. The role of the metal ion will also be investigated. Sitedirected mutagenesis studies, based on x-ray crystallographic data, will be exploited to gain further insight into the contribution of enzyme functionalities to substrate binding, monomer interface interactions and to the mechanism of the enzyme.
The emphasis of this project is to understand the mechanism(s) used by gonococci to resist antibiotic-like substances that bathe certain mucosal sites. The mtr (multiple transferable resistance)and far (fatty acid resistance) loci contain operons that encode efflux pump proteins that export structurally diverse antibacterial hydrophobic agents (HAs), including bile salts, fatty acids, lysosomal proteins and antibiotics. The MtrCDE and FarAB proteins belong to families of bacterial proteins that form efflux pumps that remove structurally diverse antimicrobial agents from either the periplasm or cytoplasm.
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