Invariom refinement of a new dimeric monoclinic 2 solvate of thiostrepton at 0.64 angstrom resolution
(2Z)-2-amino-3-sulfanylprop-2-enoic acid
8-HYDROXY-4-(1-HYDROXYETHYL)QUINOLINE-2-CARBOXYLIC ACID
(2S,3S,4R)-2-amino-3,4-dihydroxy-3-methylpentanoic acid
Invariom refinement of a new monoclinic solvate of thiostrepton at 0.64 angstrom resolution.
Alaninamide, Bryamycin, Gargon, Thiactin
DIMETHYLFORMAMID, DIETHYLETHER, pH 7.00, VAPOR DIFFUSION
THIOSTREPTON IS A MEMBER OF A SULPHUR-RICH HETEROCYCLIC PEPTIDES CLASS. ALL SHARE A MACROCYLIC CORE, CONSISTING OF A NITROGEN CONTAINING, SIX-MEMBERED RING CENTRAL TO DEHYDROAMINO ACIDS AND A SUBSET OF FIVE MEMBER RING STRUCTURES INCLUDING THIAZOLES, THIAZOLINES AND OXAZOLES. HERE, THIOSTREPTON IS REPRESENTED BY THE SEQUENCE (SEQRES)
A MODIFIED QUINOLINE QUA LINKED TO THE MAIN-CHAIN OF ILE 2 AND THE SIDE-CHAIN OF THR 13. BB9 14 INCLUDES HYDROGEN ATOM H6, THE DEHYDROPIPERIDINE CORE HYDROGEN POSITION AT THE SIX MEMBER RING SYSTEM AMONG SER 6, BB9 14 AND MH6 15.
Thiostrepton is a hetrocyclic thiopeptide belonging to the thiocillin family, consisting of four thiazole, one thiozoline and one piperideine rings. A modified quinoline linked to main-chain residue 1 and side-chain of residue 12. Post translational maturation of thiazole and oxazole containing antibiotics involves the enzymic condensation of a Cys or Ser 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. the pyridinyl 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 mutiply dehydrogenated to form a pyridine ring with loss of the amino nitrogen of the first Ser. The amidation of Ser-17 probably does not occur by the same mechanism, oxidative cleavage of glycine, as in eukaryotes.
ANTIBIOTIC, THIOPEPTIDE, ANTIBACTERIAL, THIAZOLE, THIAZOLINE, OXAZOLE, RIBOSOME, TRANSLATION INHIBITION
BINDING SITE FOR CHAIN A OF THIOSTREPTON
BINDING SITE FOR CHAIN B OF THIOSTREPTON