4cu4

FhuA from E. coli in complex with the lasso peptide microcin J25 (MccJ25)

spinqualitylabelsall models 4cu4, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4cu4 is a 2 chain structure with sequence from Escherichia coli str. k-12 substr. mc4100 and Escherichia coli mg1655. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 3PH, DAO, DPO, FTT, GCS, GMH, KDO, LDA, MYR, PA1, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [FHUA_ECOLI] This receptor binds the ferrichrome-iron ligand. It interacts with the TonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. [MCJA_ECOLX] Peptide antibiotic that functions through inhibition of the bacterial DNA-dependent RNA polymerase (RNAP). May inhibit transcription by binding in RNAP secondary channel and blocking nucleotide substrates access to the catalytic center. Exhibits potent bacteriocidal activity against a range of Enterobacteriaceae, including several pathogenic E.coli, Salmonella and Shigella strains. Also acts on the cytoplasmic membrane of Salmonella newport, producing alteration of membrane permeability and disruption of the subsequent gradient dissipation, which inhibits several processes essential for cell viability, such as oxygen consumption. Induces bacterial filamentation in susceptible cells in a non-SOS-dependent way, but this phenotype may result from impaired transcription of genes coding for cell division proteins. Publication Abstract from PubMed The lasso peptide microcin J25 is known to hijack the siderophore receptor FhuA for initiating internalization. Here, we provide what is to our knowledge the first structural evidence on the recognition mechanism, and our biochemical data show that another closely related lasso peptide cannot interact with FhuA. Our work provides an explanation on the narrow activity spectrum of lasso peptides and opens the path to the development of new antibacterials. Structural basis for hijacking siderophore receptors by antimicrobial lasso peptides.,Mathavan I, Zirah S, Mehmood S, Choudhury HG, Goulard C, Li Y, Robinson CV, Rebuffat S, Beis K Nat Chem Biol. 2014 Apr 6. doi: 10.1038/nchembio.1499. PMID:24705590 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ferric hydroxamate uptake receptor

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