PDB ID or protein name

1q71 » Microcin J25, peptide 38-58

1q71 » Microcin J25, peptide 38-58
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1q71 » Microcin J25, peptide 38-58
Hydrophobic Thickness or Depth 3.3 ± 3.2 Å
Tilt Angle 75 ± 17°
ΔGtransfer -5.2 kcal/mol
Links to 1q71 PDB Sum, PDB, SCOP, MSD, OCA, MMDB
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Resolution NMR
Other PDB entries representing this structure 1pp5
Number of subunits 1
Experimental Verification for 1q71 » Microcin J25, peptide 38-58
Due to poor solubility in water, the structure was determined in methanol. The peptide has two alternative orientations with nearly identical transfer energies: a strongly tilted and a parallel to the membrane surface. The tilted arrangement is in a better agreement with decreased fluorescence of tyrosines (Rintoul et al. 2000). There are two alternative configurations of the peptide when it interacts with uncharged phospholipid monolayers (Bellomio et al. 2005).
2 references
Bellomio A, Oliveira RG, Maggio B, Morero RD. 2005. Penetration and interactions of the antimicrobial peptide, microcin J25, into uncharged phospholipid monolayers. J Colloid Interface Sci. 285:118-24. PubMed
Rintoul MR, de Arcuri BF, Morero RD. 2000. Effects of the antibiotic peptide microcin J25 on liposomes: role of acyl chain length and negatively charged phospholipid. Biochim Biophys Acta. 1509:65-72. PubMed
Comments on 1q71 » Microcin J25, peptide 38-58
Peptide antibiotic that functions through inhibition of the bacterial DNA-dependent RNA polymerase (RNAP). 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.