General Information

    • DRAMP ID

    • DRAMP02471

    • Peptide Name

    • Thiostrepton (Alaninamide; Bryamycin; Gargon; Thiactin)

    • Source

    • Streptomyces azureus

    • Family

    • Belongs to the thiocillin family

    • Gene

    • tpdA

    • Sequence

    • IASASCTTCICTCSCSS

    • Sequence Length

    • 17

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial

    • Target Organism

    • No MICs found in DRAMP database

    • Hemolytic Activity

      • No hemolysis information or data found in the reference(s) presented in this entry

    • Cytotoxicity

      • Not included yet

    • Binding Target

    • Not found

Structure Information

    • Linear/Cyclic

    • Not included yet

    • N-terminal Modification

    • Not included yet

    • C-terminal Modification

    • Not included yet

    • Nonterminal Modifications and Unusual Amino Acids

    • Not included yet

    • Stereochemistry

    • Not included yet

    • Structure

    • No secondary structure

    • Structure Description

    • Not found

    • Helical Wheel Diagram

    • DRAMP02471 helical wheel diagram
  • 1E9W-> 

    • Predicted Structure

    • There is no predicted structure for DRAMP02471.

Physicochemical Information

    • Formula

    • C60H105N17O26S5

    • Absent Amino Acids

    • DEFGHKLMNPQRVWY

    • Common Amino Acids

    • CS

    • Mass

    • 1640.89

    • PI

    • 5.49

    • Basic Residues

    • 0

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 4

    • Net Charge

    • 0

    • Boman Index

    • -4.85

    • Hydrophobicity

    • 1.118

    • Aliphatic Index

    • 57.65

    • Half Life

      • Mammalian:20 hour
      • Yeast:30 min
      • E.coli:>10 hour

    • Extinction Coefficient Cystines

    • 250

    • Absorbance 280nm

    • 15.63

    • Polar Residues

    • 13

DRAMP02471

Comments Information

    • Function

    • Has bacteriocidal activity. Inhibits bacterial protein biosynthesis by acting on the elongation factor Tu (EF-Tu) (By similarity).

    • PTM

    • Maturation of thiazole and oxazole containing antibiotics involves the enzymic condensation of a Cys, Ser or Thr with the alpha-carbonyl of the preceding amino acid to form a thioether or ether bond, then dehydration to form a double bond with the alpha-amino nitrogen. Thiazoline or oxazoline ring are dehydrogenated to form thiazole or oxazole rings. Maturation of pyridinyl containing antibiotics involves the cross-linking of a Ser and a Cys-Ser pair usually separated by 7 or 8 residues along the peptide chain. The Ser residues are dehydrated to didehydroalanines, then bonded between their beta carbons. The alpha carbonyl of the Cys condenses with alpha carbon of the first Ser to form a pyridinyl ring. The ring may be multiply dehydrogenated to form a pyridine ring with loss of the amino nitrogen of the first Ser.

    • Pharmaceutical use

    • Available under the names Animax (Dechra) and Panolog (Fort Dodge), that combine thiostrepton with nystatin (antifungal), neomycin (antibiotic) and triamcinolone (corticosteroid). Used to treat cat and dog skin and ear disorders caused by

Literature Information

  • ·Literature 1

    • Title

    • Thiostrepton, a new antibiotic. I. In vitro studies.

    • Reference

    • Antibiot Annu. 1955-1956;3:554-559.

    • Author

    • DONOVICK R, PAGANO JF, STOUT HA, WEINSTEIN MJ.
  • ·Literature 2

    • Title

    • Structure of the macrocycle thiostrepton solved using the anomalous dispersion contribution of sulfur.

    • Reference

    • Acta Crystallogr D Biol Crystallogr. 2001 May;57(Pt 5):755-758.

    • Author

    • Bond CS, Shaw MP, Alphey MS, Hunter WN.