1s7p
From Proteopedia
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{{STRUCTURE_1s7p| PDB=1s7p | SCENE= }} | {{STRUCTURE_1s7p| PDB=1s7p | SCENE= }} | ||
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===Solution structure of thermolysin digested microcin J25=== | ===Solution structure of thermolysin digested microcin J25=== | ||
| + | {{ABSTRACT_PUBMED_15096038}} | ||
| - | + | ==Function== | |
| - | + | [[http://www.uniprot.org/uniprot/MCJA_ECOLI MCJA_ECOLI]] 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.<ref>PMID:11731133</ref> <ref>PMID:11443089</ref> <ref>PMID:12401787</ref> | |
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==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:015096038</ref><references group="xtra"/> | + | <ref group="xtra">PMID:015096038</ref><references group="xtra"/><references/> |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Afonso, C.]] | [[Category: Afonso, C.]] | ||
Revision as of 08:16, 23 April 2014
Contents |
Solution structure of thermolysin digested microcin J25
Template:ABSTRACT PUBMED 15096038
Function
[MCJA_ECOLI] 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.[1] [2] [3]
About this Structure
1s7p is a 2 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA.
Reference
- Rosengren KJ, Blond A, Afonso C, Tabet JC, Rebuffat S, Craik DJ. Structure of thermolysin cleaved microcin J25: extreme stability of a two-chain antimicrobial peptide devoid of covalent links. Biochemistry. 2004 Apr 27;43(16):4696-702. PMID:15096038 doi:10.1021/bi0361261
- ↑ 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
