7k5h

1.90 A resolution structure of WT BfrB from Pseudomonas aeruginosa in complex with a protein-protein interaction inhibitor KM-5-66

spinqualitylabelsall models 7k5h, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: HEM, K, VXV Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Bacteria depend on a well-regulated iron homeostasis to survive adverse environments. A key component of the iron homeostasis machinery is the compartmentalization of Fe(3+) in bacterioferritin and its subsequent mobilization as Fe(2+) to satisfy metabolic requirements. In Pseudomonas aeruginosa Fe(3+) is compartmentalized in bacterioferritin (BfrB), and its mobilization to the cytosol requires binding of a ferredoxin (Bfd) to reduce the stored Fe(3+) and release the soluble Fe(2+). Blocking the BfrB-Bfd complex in P. aeruginosa by deletion of the bfd gene triggers an irreversible accumulation of Fe(3+) in BfrB, concomitant cytosolic iron deficiency and significant impairment of biofilm development. Herein we report that small molecules developed to bind BfrB at the Bfd binding site block the BfrB-Bfd complex, inhibit the mobilization of iron from BfrB in P. aeruginosa cells, elicit a bacteriostatic effect on planktonic cells, and are bactericidal to cells embedded in mature biofilms. Small Molecule Inhibitors of the Bacterioferritin (BfrB)-Ferredoxin (Bfd) Complex Kill Biofilm-Embedded Pseudomonas aeruginosa Cells.,Soldano A, Yao H, Punchi Hewage AND, Meraz K, Annor-Gyamfi JK, Bunce RA, Battaile KP, Lovell S, Rivera M ACS Infect Dis. 2020 Dec 3. doi: 10.1021/acsinfecdis.0c00669. PMID:33269912 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ferritin 3D structures

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