2N2L
NMR structure of yersinia pestis ail (attachment invasion locus) in decylphosphocholine micelles calculated with implicit membrane solvation
Summary for 2N2L
| Entry DOI | 10.2210/pdb2n2l/pdb |
| Related | 2N2M |
| Descriptor | Outer membrane protein X (1 entity in total) |
| Functional Keywords | membrane protein |
| Biological source | Yersinia pestis |
| Total number of polymer chains | 1 |
| Total formula weight | 17492.40 |
| Authors | Marassi, F.M.,Ding, Y.,Tian, Y.,Schwieters, C.D.,Yao, Y. (deposition date: 2015-05-10, release date: 2015-07-22, Last modification date: 2024-05-15) |
| Primary citation | Marassi, F.M.,Ding, Y.,Schwieters, C.D.,Tian, Y.,Yao, Y. Backbone structure of Yersinia pestis Ail determined in micelles by NMR-restrained simulated annealing with implicit membrane solvation. J.Biomol.Nmr, 63:59-65, 2015 Cited by PubMed Abstract: 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. PubMed: 26143069DOI: 10.1007/s10858-015-9963-2 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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