首页    期刊浏览 2025年07月13日 星期日
登录注册

文章基本信息

  • 标题:C-Mannosylation Enhances the Structural Stability of Human RNase 2
  • 本地全文:下载
  • 作者:Martin Frank ; Daniela Beccati ; Bas R. Leeflang
  • 期刊名称:iScience
  • 印刷版ISSN:2589-0042
  • 出版年度:2020
  • 卷号:23
  • 期号:8
  • 页码:1-30
  • DOI:10.1016/j.isci.2020.101371
  • 语种:English
  • 出版社:Elsevier
  • 摘要:SummaryC-Mannosylation is a relatively rare form of protein glycosylation involving the attachment of an α-mannopyranosyl residue to C-2 of the indole moiety of the amino acid tryptophan. This type of linkage was initially discovered in RNase 2 from human urine but later confirmed to be present in many other important proteins. Based on NMR experiments and extensive molecular dynamics simulations on the hundred microsecond timescale we demonstrate that, for isolated glycopeptides and denatured RNase 2, the C-linked mannopyranosyl residue exists as an ensemble of conformations, among which1C4is the most abundant. However, for native RNase 2, molecular dynamics and NMR studies revealed that the mannopyranosyl residue favors a specific conformation, which optimally stabilizes the protein fold through a network of hydrogen bonds and which leads to a significant reduction of the protein dynamics on the microsecond timescale. Our findings contribute to the understanding of the biological role ofC-mannosylation.Graphical AbstractDisplay OmittedHighlights•NMR and MD show thatC-linked mannose exists as an ensemble of conformations•Conformation of mannose is influenced by the protein environment and solvent•In RNase 2 mannose favors a conformation that optimally stabilizes the protein fold•Efficient methods for analysis of a large number of MD trajectories are presentedBiochemistry; Structural Biology; Protein Structure Aspects
国家哲学社会科学文献中心版权所有