5FR3

X-ray crystal structure of aggregation-resistant protective antigen of Bacillus anthracis (mutant S559L T576E)

5FR3 の概要

• エントリーDOI: 10.2210/pdb5fr3/pdb
• 分子名称: PROTECTIVE ANTIGEN, CALCIUM ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: toxin, anthrax protective antigen
• 由来する生物種: BACILLUS ANTHRACIS
• 細胞内の位置: Secreted, extracellular space: P13423
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 81515.57

構造登録者

Ganesan, A.,Siekierska, A.,Beerten, J.,Brams, M.,van Durme, J.,De Baets, G.,van der Kant, R.,Gallardo, R.,Ramakers, M.,Langenberg, T.,Wilkinson, H.,De Smet, F.,Ulens, C.,Rousseau, F.,Schymkowitz, J. (登録日: 2015-12-15, 公開日: 2016-01-27, 最終更新日: 2024-01-10)

主引用文献

Ganesan, A.,Siekierska, A.,Beerten, J.,Brams, M.,Van Durme, J.,De Baets, G.,Van Der Kant, R.,Gallardo, R.,Ramakers, M.,Langenberg, T.,Wilkinson, H.,De Smet, F.,Ulens, C.,Rousseau, F.,Schymkowitz, J.
Structural Hot Spots for the Solubility of Globular Proteins
Nat.Commun., 7:10816-, 2016

PubMed Abstract: Natural selection shapes protein solubility to physiological requirements and recombinant applications that require higher protein concentrations are often problematic. This raises the question whether the solubility of natural protein sequences can be improved. We here show an anti-correlation between the number of aggregation prone regions (APRs) in a protein sequence and its solubility, suggesting that mutational suppression of APRs provides a simple strategy to increase protein solubility. We show that mutations at specific positions within a protein structure can act as APR suppressors without affecting protein stability. These hot spots for protein solubility are both structure and sequence dependent but can be computationally predicted. We demonstrate this by reducing the aggregation of human α-galactosidase and protective antigen of Bacillus anthracis through mutation. Our results indicate that many proteins possess hot spots allowing to adapt protein solubility independently of structure and function.

PubMed: 26905391
DOI: 10.1038/NCOMMS10816

実験手法

X-RAY DIFFRACTION (1.935 Å)