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Additional resources for Devil's Domain; Villains and Vigilantes 2014
42 VolkmarBraun, MichaelBraun and Helmut Killmann 2. , 1998, Structure of the Shigella dysenteriae haem transport locus and its phylogenetic distribution in enteric bacteria. Mol. Microbiol. 28: 1139–1152. 3. , 1996, Periplasmic binding protein-dependent ABC transporters. In Escherichia coli and Salmonella. C. ) ASM Press, Washington. pp. 1175–1209. 4. , 1997, ATP-dependent ferric hydroxamate transport system in Escherichia coli: periplasmic FhuD interacts with a periplasmic and with a transmembrane/cytoplasmic region of the integral membrane protein FhuB, as revealed by competitive peptide mapping.
Therefore, it was particularly attractive to determine the crystal structure of FhuA loaded with CGP483219. Analysis of the X-ray diffraction data revealed that CGP 4832 largely occupies the site in FhuA that is also used by ferrichrome. Interestingly, three amino acid residues, which also bind ferrichrome, recognize those side chains of CGP 4832 that differ from unmodified rifamycin (Fig 2). Two unique residues also contact such CGP 4832 side chains, whereas the 12 residues bind to sites that CGP 4832 shares with rifamycin.
Immunohistochemistry identified the kidney epithelium as a main source of MIP-2. MIP-2 antibody treatment of the mice caused the neutrophils to aggregate under the pelvic epithelium, but in control mice the neutrophils crossed the urothelium into the urine. The results demonstrate that MIP-2 directs neutrophil migration through the lamina propria and across the epithelium. Neutrophils cross the epithelial cell barriers in a highly regulated manner, in response to chemokines elaborated at this site.