Structure of the macrocycle thiostrepton solved using the anomalous dispersive contribution from sulfur
(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
1ML 15.38MG/ML THIOSTREPTON IN CHLOROFORM_ISOAMYL ALCOHOL + 100 MICROL GLYCEROL + 200 MICROL ETHANOL. BATCH METHOD, pH 7.00
CRYSTAL STRUCTURE OF THE ELONGATION FACTOR EF-TU-MGGDP COMPLEXED WITH THE THIOPEPTIDE GE2270A.
SOLUTION STRUCTURE OF THIOPEPTIDE THIOSTREPTON BINDING TO L11 SUBSTRATE FROM 50S RIBOSOMAL RNA
CRYSTAL STRUCTURE OF THE ELONGATION FACTOR EF-TU-GNP COMPLEXED WITH THIOPEPTIDE GE2270A.
SOLUTION STRUCTURE OF THE COMPLEX OF THE THIOPEPTIDE THIOSTREPTON AND RIBOSOMAL L11-RNA
CRYSTAL STRUCTURE OF NOSIHEPTIDE COMPLEXED WITH THE LARGE RIBOSOMAL SUBUNIT OF DEINOCOCCUS RADIODURANS
CRYSTAL STRUCTURE OF RIBOSOMAL L11-RNA COMPLEXED WITH THE THIOPEPTIDE THIOSTREPTON
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) GROUP: 1 NAME: THIOSTREPTON CHAIN: A COMPONENT_1: PEPTIDE LIKE SEQUENCE RESIDUES 0 TO 18 DESCRIPTION: THIOSTREPTON IS A HETROCYCLIC THIOPEPTIDE, CONSISTING OF FOUR THIAZOLES ONE THIOZOLINE ONE PIPERIDEINE RINGS. A MODIFIED QUINOLINE LINKED TO MAIN-CHAIN RESIDUE 1 AND SIDE-CHAIN OF RESIDUE 12. THE OBSERVED C-TERMINAL AMINO GROUP NH2(18) IS LIKELY TO BE A POST-TRANSLATIONAL DECARBOXYLATED REMNANT OF A SER C-TERMINAL RESIDUE
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.
RESIDUE 16 RESTRAINED USING GEOMETRY DERIVED FROM CSD (SEE REFERENCE)
MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-2
ANTIBIOTIC, THIOPEPTIDE, ANTIBACTERIAL, THIAZOLE, THIAZOLINE, OXAZOLE, RIBOSOME, TRANSLATION INHIBITION
BINDING SITE FOR CHAIN A OF THIOSTREPTON