Backbone structure of Yersinia pestis Ail determined in micelles by NMR-restrained simulated annealing with implicit membrane solvation. J Biomol NMR 2015 Sep;63(1):59-65
Date
07/06/2015Pubmed ID
26143069Pubmed Central ID
PMC4577439DOI
10.1007/s10858-015-9963-2Scopus ID
2-s2.0-84942374186 (requires institutional sign-in at Scopus site) 21 CitationsAbstract
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.
Author List
Marassi FM, Ding Y, Schwieters CD, Tian Y, Yao YAuthor
Francesca M. Marassi PhD Chair, Professor in the Biophysics department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Bacterial Outer Membrane ProteinsCell Membrane
Computer Simulation
Micelles
Models, Molecular
Nuclear Magnetic Resonance, Biomolecular
Phosphorylcholine
Reproducibility of Results
Solvents
Virulence Factors
Yersinia pestis
