6MY1

Solution structure of gomesin at 278 K

6MY1 の概要

• エントリーDOI: 10.2210/pdb6my1/pdb
• 関連するPDBエントリー: 1KFP 6MY2 6MY3
• NMR情報: BMRB: 30534
• 分子名称: gomesin (1 entity in total)
• 機能のキーワード: peptides, beta hairpin motif, toxin
• 由来する生物種: Acanthoscurria gomesiana
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2279.76

構造登録者

Chin, Y.K.-Y.,Deplazes, E. (登録日: 2018-10-31, 公開日: 2019-11-06, 最終更新日: 2024-11-20)

主引用文献

Deplazes, E.,Chin, Y.K.,King, G.F.,Mancera, R.L.
The unusual conformation of cross-strand disulfide bonds is critical to the stability of beta-hairpin peptides.
Proteins, 88:485-502, 2020

PubMed Abstract: The cross-strand disulfides (CSDs) found in β-hairpin antimicrobial peptides (β-AMPs) show a unique disulfide geometry that is characterized by unusual torsion angles and a short Cα-Cα distance. While the sequence and disulfide bond connectivity of disulfide-rich peptides is well studied, much less is known about the disulfide geometry found in CSDs and their role in the stability of β-AMPs. To address this, we solved the nuclear magnetic resonance (NMR) structure of the β-AMP gomesin (Gm) at 278, 298, and 310 K, examined the disulfide bond geometry of over 800 disulfide-rich peptides, and carried out extensive molecular dynamics (MD) simulation of the peptides Gm and protegrin. The NMR data suggests Cα-Cα distances characteristic for CSDs are independent of temperature. Analysis of disulfide-rich peptides from the Protein Data Bank revealed that right-handed and left-handed rotamers are equally likely in CSDs. The previously reported preference for right-handed rotamers was likely biased by restricting the analysis to peptides and proteins solved using X-ray crystallography. Furthermore, data from MD simulations showed that the short Cα-Cα distance is critical for the stability of these peptides. The unique disulfide geometry of CSDs poses a challenge to biomolecular force fields and to retain the stability of β-hairpin fold over long simulation times, restraints on the torsion angles might be required.

PubMed: 31589791
DOI: 10.1002/prot.25828

実験手法

SOLUTION NMR