ジャーナル: Biochemistry / 年: 2000 タイトル: Structure of an EF-TU Complex with a Thiazolyl Peptide Antibiotic Determined at 2.35 A Resolution: Atomic Basis for Ge2270A Inhibition of EF-TU. 著者: Heffron, S.E. / Jurnak, F.
履歴
登録
1999年10月25日
登録サイト: RCSB / 処理サイト: RCSB
改定 1.0
2000年10月25日
Provider: repository / タイプ: Initial release
改定 1.1
2011年6月14日
Group: Version format compliance
改定 1.2
2011年7月13日
Group: Version format compliance
改定 1.3
2011年7月27日
Group: Atomic model / Database references ...Atomic model / Database references / Derived calculations / Non-polymer description / Structure summary
SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AG" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AG" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "BG" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.
タイプ: Thiopeptideチオペプチド / クラス: 抗生剤抗生物質 / 分子量: 1484.681 Da / 分子数: 2 / 由来タイプ: 天然 詳細: GEA2270A IS A THIOPEPTIDE CONSISTING OF ONE PYRIDINE, ONE OXAZOLE AND FIVE THIAZOLE RINGS. THE OBSERVED C-TERMINAL AMINO GROUP NH2(15) IS LIKELY TO BE A POST-TRANSLATIONAL DECARBOXYLATED ...詳細: GEA2270A IS A THIOPEPTIDE CONSISTING OF ONE PYRIDINE, ONE OXAZOLE AND FIVE THIAZOLE RINGS. THE OBSERVED C-TERMINAL AMINO GROUP NH2(15) IS LIKELY TO BE A POST-TRANSLATIONAL DECARBOXYLATED REMNANT OF A SER C-TERMINAL RESIDUE. 由来: (天然) PLANOBISPORA ROSEA (バクテリア) / 参照: UniProt: Q7M0J8, GE2270a
GEA2270A is a member of a sulphur-rich heterocyclic peptides class. All members share a macrocylic ...GEA2270A is a member of a sulphur-rich heterocyclic peptides class. All members 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. 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. In addition cross-linking of a Ser and a Cys-Ser pair usually separated by 7 or 8 residues along the peptide chain produce a pyridinyl ring. 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. Several isomers are produced. The structural differences between them lie in the extent of the modifications, methylation, methoxylation, and oxidation of the thiazole and oxazole rings, and methylation of asparagine. The amidation of Pro-14 probably does not occur by the same mechanism, oxidative cleavage of glycine, as in eukaryotes.