5MAS

Peptaibol Bergofungin A

5MAS の概要

• エントリーDOI: 10.2210/pdb5mas/pdb
• 関連するPDBエントリー: 4G13 4G14
• 分子名称: Bergofungin A (2 entities in total)
• 機能のキーワード: 3(10)-helix, peptaibols, antibiotic peptides, alpha-helix, antibiotic
• 由来する生物種: Emericellopsis donezkii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1509.83

構造登録者

Gessmann, R.,Petratos, K. (登録日: 2016-11-04, 公開日: 2017-02-22, 最終更新日: 2025-04-09)

主引用文献

Gessmann, R.,Axford, D.,Bruckner, H.,Berg, A.,Petratos, K.
A natural, single-residue substitution yields a less active peptaibiotic: the structure of bergofungin A at atomic resolution.
Acta Crystallogr F Struct Biol Commun, 73:95-100, 2017

PubMed Abstract: Bergofungin is a peptide antibiotic that is produced by the ascomycetous fungus Emericellopsis donezkii HKI 0059 and belongs to peptaibol subfamily 2. The crystal structure of bergofungin A has been determined and refined to 0.84 Å resolution. This is the second crystal structure of a natural 15-residue peptaibol, after that of samarosporin I. The amino-terminal phenylalanine residue in samarosporin I is exchanged to a valine residue in bergofungin A. According to agar diffusion tests, this results in a nearly inactive antibiotic peptide compared with the moderately active samarosporin I. Crystals were obtained from methanol solutions of purified bergofungin mixed with water. Although there are differences in the intramolecular hydrogen-bonding scheme of samarosporin I, the overall folding is very similar for both peptaibols, namely 3-helical at the termini and α-helical in the middle of the molecules. Bergofungin A and samarosporin I molecules are arranged in a similar way in both lattices. However, the packing of bergofungin A exhibits a second solvent channel along the twofold axis. This latter channel occurs in the vicinity of the N-terminus, where the natural substitution resides.

PubMed: 28177320
DOI: 10.1107/S2053230X17001236

実験手法

X-RAY DIFFRACTION (0.84 Å)