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 mg1655 and Escherichia coli str. k-12 substr. mc4100. Full crystallographic information is available from OCA.

Ligands: , , , , , , , , ,
NonStd Res:
Activity: Glucokinase, with EC number 2.7.1.2
Resources: FirstGlance, OCA, RCSB, PDBsum

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Mathavan I, Zirah S, Mehmood S, Choudhury HG, Goulard C, Li Y, Robinson CV, Rebuffat S, Beis K. Structural basis for hijacking siderophore receptors by antimicrobial lasso peptides. Nat Chem Biol. 2014 Apr 6. doi: 10.1038/nchembio.1499. PMID:24705590 doi:http://dx.doi.org/10.1038/nchembio.1499

4cu4, resolution 2.30Å

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