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4CU4

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

Summary for 4CU4
Entry DOI10.2210/pdb4cu4/pdb
Related PRD IDPRD_000184
DescriptorFERRICHROME-IRON RECEPTOR, PHOSPHATE ION, MICROCIN J25, ... (11 entities in total)
Functional Keywordstransport protein-antibiotic complex, lipopolysaccharide, detergent, transport protein/antibiotic
Biological sourceESCHERICHIA COLI STR. K-12 SUBSTR. MG1655
More
Total number of polymer chains2
Total formula weight88629.36
Authors
Mathavan, I.,Rebuffat, S.,Beis, K. (deposition date: 2014-03-17, release date: 2014-04-09, Last modification date: 2024-11-13)
Primary citationMathavan, I.,Zirah, S.,Mehmood, S.,Choudhury, H.G.,Goulard, C.,Li, Y.,Robinson, C.V.,Rebuffat, S.,Beis, K.
Structural Basis for Hijacking Siderophore Receptors by Antimicrobial Lasso Peptides.
Nat.Chem.Biol., 10:340-, 2014
Cited by
PubMed Abstract: 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.
PubMed: 24705590
DOI: 10.1038/NCHEMBIO.1499
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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