4G13

Crystal structure of samarosporin I at 100K

4G13 の概要

• エントリーDOI: 10.2210/pdb4g13/pdb
• 関連するPDBエントリー: 1JOH 1OB4 1OB6 1OB7 4G14
• 関連するBIRD辞書のPRD_ID: PRD_000920
• 分子名称: SAMAROSPORIN I (2 entities in total)
• 機能のキーワード: peptaibol, 3(10)-alpha helix, antibiotic peptide, membrane, extracellular, antibiotic
• 由来する生物種: samarospora rostrup
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1557.88

構造登録者

Gessmann, R.,Axford, D.,Petratos, K. (登録日: 2012-07-10, 公開日: 2012-10-03, 最終更新日: 2018-07-18)

主引用文献

Gessmann, R.,Axford, D.,Evans, G.,Bruckner, H.,Petratos, K.
The crystal structure of samarosporin I at atomic resolution.
J.Pept.Sci., 18:678-684, 2012

PubMed Abstract: The atomic resolution structures of samarosporin I have been determined at 100 and 293 K. This is the first crystal structure of a natural 15-residue peptaibol. The amino acid sequence in samarosporin I is identical to emerimicin IV and stilbellin I. Samarosporin is a peptide antibiotic produced by the ascomycetous fungus Samarospora rostrup and belongs to peptaibol subfamily 2. The structures at both temperatures are very similar to each other adopting mainly a 3₁₀-helical and a minor fraction of α-helical conformation. The helices are significantly bent and packed in an antiparallel fashion in the centered monoclinic lattice leaving among them an approximately 10-Å channel extending along the crystallographic twofold axis. Only two ordered water molecules per peptide molecule were located in the channel. Comparisons have been carried out with crystal structures of subfamily 2 16-residue peptaibols antiamoebin and cephaibols. The repercussion of the structural analysis of samarosporin on membrane function is discussed.

PubMed: 23019149
DOI: 10.1002/psc.2454

実験手法

X-RAY DIFFRACTION (0.8 Å)