Backbone structure of Yersinia pestis Ail determined in micelles by NMR-restrained simulated annealing with implicit membrane solvation

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• 作者：Francesca M. Marassi ; Yi Ding ; Charles D. Schwieters…
• 关键词：Ail ; Yersinia pestis ; Membrane protein ; Structure ; NMR ; Implicit solvation
• 刊名：Journal of Biomolecular NMR
• 出版年：2015
• 出版时间：September 2015
• 年：2015
• 卷：63
• 期：1
• 页码：59-65
• 全文大小：717 KB
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• 作者单位：Francesca M. Marassi (1)
  Yi Ding (1)
  Charles D. Schwieters (2)
  Ye Tian (1)
  Yong Yao (1)
  
  1. Sanford-Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, CA, 92037, USA
  2. Division of Computational Bioscience, Center for Information Technology, National Institutes of Health, Building 12A, Bethesda, MD, 20892-5624, USA
  
• 刊物类别：Physics and Astronomy
• 刊物主题：Physics
  Biophysics and Biomedical Physics
  Polymer Sciences
  Biochemistry
  
• 出版者：Springer Netherlands
• ISSN：1573-5001

文摘

The outer membrane protein Ail (attachment invasion locus) is a virulence factor of Yersinia pestis that mediates cell invasion, cell attachment and complement resistance. Here we describe its three-dimensional backbone structure determined in decyl-phosphocholine (DePC) micelles by NMR spectroscopy. The NMR structure was calculated using the membrane function of the implicit solvation potential, eefxPot, which we have developed to facilitate NMR structure calculations in a physically realistic environment. We show that the eefxPot force field guides the protein towards its native fold. The resulting structures provide information about the membrane-embedded global position of Ail, and have higher accuracy, higher precision and improved conformational properties, compared to the structures calculated with the standard repulsive potential. Keywords Ail Yersinia pestis Membrane protein Structure NMR Implicit solvation