4cu4: Difference between revisions
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{{STRUCTURE_4cu4| PDB=4cu4 | SCENE= }} | {{STRUCTURE_4cu4| PDB=4cu4 | SCENE= }} | ||
===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)=== | ||
{{ABSTRACT_PUBMED_24705590}} | |||
==Function== | ==Function== | ||
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==Reference== | ==Reference== | ||
<references group="xtra"/><references/> | <ref group="xtra">PMID:024705590</ref><references group="xtra"/><references/> | ||
[[Category: Escherichia coli str. k-12 substr. mc4100]] | [[Category: Escherichia coli str. k-12 substr. mc4100]] | ||
[[Category: Beis, K.]] | [[Category: Beis, K.]] | ||
Revision as of 10:30, 16 April 2014
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)
Template:ABSTRACT PUBMED 24705590
FunctionFunction
[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.[1] [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.[2] [3] [4]
About this StructureAbout this Structure
4cu4 is a 2 chain structure with sequence from [1] and Escherichia coli str. k-12 substr. mc4100. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ 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
- ↑ Bonhivers M, Ghazi A, Boulanger P, Letellier L. FhuA, a transporter of the Escherichia coli outer membrane, is converted into a channel upon binding of bacteriophage T5. EMBO J. 1996 Apr 15;15(8):1850-6. PMID:8617231
- ↑ Rintoul MR, de Arcuri BF, Salomon RA, Farias RN, Morero RD. The antibacterial action of microcin J25: evidence for disruption of cytoplasmic membrane energization in Salmonella newport. FEMS Microbiol Lett. 2001 Nov 13;204(2):265-70. PMID:11731133
- ↑ Delgado MA, Rintoul MR, Farias RN, Salomon RA. Escherichia coli RNA polymerase is the target of the cyclopeptide antibiotic microcin J25. J Bacteriol. 2001 Aug;183(15):4543-50. PMID:11443089 doi:http://dx.doi.org/10.1128/JB.183.15.4543-4550.2001
- ↑ Yuzenkova J, Delgado M, Nechaev S, Savalia D, Epshtein V, Artsimovitch I, Mooney RA, Landick R, Farias RN, Salomon R, Severinov K. Mutations of bacterial RNA polymerase leading to resistance to microcin j25. J Biol Chem. 2002 Dec 27;277(52):50867-75. Epub 2002 Oct 24. PMID:12401787 doi:http://dx.doi.org/10.1074/jbc.M209425200