4cu4

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

Structural highlights 4cu4 is a 2 chain structure with sequence from Escherichia coli str. K-12 substr. MC4100 and Escherichia coli str. K-12 substr. MG1655. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: , , , , , , , , , , 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. 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

spinqualitylabelsall models 4cu4, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image