View bacteriocin : Actagardine (Gardimycin)

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Accession BAC012
Name Actagardine (Gardimycin)
Gene Unidentified
Class Lantibiotic
Producer Organism Actinoplanes liguriae [Gram-positive]
Taxonomy BacteriaActinobacteriaActinobacteridaeActinomycetalesMicromonosporineaeMicromonosporaceaeActinoplanes
Target organisms Gram-positive bacteria -

Has good antistreptococcal activity: streptococci - Streptococcus pyogenes
Swiss-Prot Entry P56650
PDB Entry 1AJ1 resolved by NMR
Other databases PIR A58700
Description Mode of action:
Lanthionine-containing peptide antibiotic (lantibiotic). The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores.

Post-translational modification:
Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. The 14-19 beta-methyllanthionine thioether bond is oxidized to a sulfoxide. This is followed by membrane translocation and cleavage of the modified precursor.
[Ref. 1] | View abstract | Export citation
PRELIMINARY PROTEIN SEQUENCE, AND STRUCTURE BY NMR.
MEDLINE=91008698;PubMed=2211371;
Kettenring J.K., Malabarba A., Vekey K., Cavalleri B.
"Sequence determination of actagardine, a novel lantibiotic, by homonuclear 2D NMR spectroscopy.", J. Antibiot. 43:1082-1088(1990).

[Ref. 2] | View abstract | Export citation
PROTEIN SEQUENCE, AND STRUCTURE BY NMR.
MEDLINE=95255286;PubMed=7737178;
Zimmermann N., Metzger J.W., Jung G.
"The tetracyclic lantibiotic actagardine. 1H-NMR and 13C-NMR assignments and revised primary structure.", Eur. J. Biochem. 228:786-797(1995).

[Ref. 3] | View abstract | Export citation
STRUCTURE BY NMR.
MEDLINE=97363218;PubMed=9219543;
Zimmermann N., Jung G.
"The three-dimensional solution structure of the lantibiotic murein- biosynthesis-inhibitor actagardine determined by NMR.", Eur. J. Biochem. 246:809-819(1997).

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Sequence
 ........10 ........20 
          |          | 
 SSGWVCTLTI ECGTVICAC

Wheel representation
Structure
Composition
Formula C81 H132 N20 O27 S4
Absent amino acids DFHKMNPQRY
Common amino acids C
Mass (Da) 1964.62
Net charge -1
Isoelectric point 3.85
Basic residues 0
Acidic residues 1
Hydrophobic residues 7
Polar residues 11
Aliphatic residues 5
Tiny residues 5
Boman Index 12.66
Hydropathy Index 1.27
Aliphatic Index 97.37
Instability Index 103.71 (unstable)
Half Life Mammalian : 1.9 hour
Yeast : >20 hour
E. coli : >10 hour
Extinction Coefficient 5750 M-1 cm-1
Absorbance 280nm 319.44
Red solid plot : values according to the hydrophobicity scale of Kyte and Doolittle (reference paper).


Yellow dashed plot : Experimentally determined hydrophobicity scale for proteins at membrane interfaces(reference paper).


Green dotted-dashed plot : prediction of transmembrane helices (reference paper). In this scale (unlike the others), more negative values reflect greater hydrophobicity.

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