3E7R

X-ray Crystal Structure of Racemic Plectasin

3E7R の概要

• エントリーDOI: 10.2210/pdb3e7r/pdb
• 関連するPDBエントリー: 3E7U
• 分子名称: Plectasin (2 entities in total)
• 機能のキーワード: plectasin, racemic protein crystallography, antibiotic, antimicrobial, cleavage on pair of basic residues, defensin, secreted, antimicrobial protein
• 細胞内の位置: Secreted (Probable): Q53I06
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4415.02

構造登録者

Mandal, K.,Pentelute, B.L.,Tereshko, V.,Kossiakoff, A.A.,Kent, S.B.H. (登録日: 2008-08-18, 公開日: 2009-06-09, 最終更新日: 2024-10-16)

主引用文献

Mandal, K.,Pentelute, B.L.,Tereshko, V.,Thammavongsa, V.,Schneewind, O.,Kossiakoff, A.A.,Kent, S.B.
Racemic crystallography of synthetic protein enantiomers used to determine the X-ray structure of plectasin by direct methods
Protein Sci., 18:1146-1154, 2009

PubMed Abstract: We describe the use of racemic crystallography to determine the X-ray structure of the natural product plectasin, a potent antimicrobial protein recently isolated from fungus. The protein enantiomers L-plectasin and D-plectasin were prepared by total chemical synthesis; interestingly, L-plectasin showed the expected antimicrobial activity, while D-plectasin was devoid of such activity. The mirror image proteins were then used for racemic crystallization. Synchrotron X-ray diffraction data were collected to atomic resolution from a racemic plectasin crystal; the racemate crystallized in the achiral centrosymmetric space group P1 with one L-plectasin molecule and one D-plectasin molecule forming the unit cell. Dimer-like intermolecular interactions between the protein enantiomers were observed, which may account for the observed extremely low solvent content (13%-15%) and more highly ordered nature of the racemic crystals. The structure of the plectasin molecule was well defined for all 40 amino acids and was generally similar to the previously determined NMR structure, suggesting minimal impact of the crystal packing on the plectasin conformation.

PubMed: 19472324
DOI: 10.1002/pro.127

実験手法

X-RAY DIFFRACTION (1 Å)