5VJ8
Backbone structure of the Yersinia pestis outer membrane protein Ail in phospholipid bilayer nanodisc
Summary for 5VJ8
| Entry DOI | 10.2210/pdb5vj8/pdb |
| Related | 2n2l |
| NMR Information | BMRB: 30284 |
| Descriptor | Adhesion invasion locus (1 entity in total) |
| Functional Keywords | adhesion invasion locus, nanodisc, membrane protein, beta-barrel |
| Biological source | Yersinia pestis |
| Total number of polymer chains | 1 |
| Total formula weight | 17492.40 |
| Authors | Dutta, S.K.,Yong, Y.,Marassi, F.M. (deposition date: 2017-04-19, release date: 2017-05-17, Last modification date: 2024-05-15) |
| Primary citation | Dutta, S.K.,Yao, Y.,Marassi, F.M. Structural Insights into the Yersinia pestis Outer Membrane Protein Ail in Lipid Bilayers. J Phys Chem B, 121:7561-7570, 2017 Cited by PubMed Abstract: Yersinia pestis the causative agent of plague, is highly pathogenic and poses very high risk to public health. The outer membrane protein Ail (Adhesion invasion locus) is one of the most highly expressed proteins on the cell surface of Y. pestis, and a major target for the development of medical countermeasures. Ail is essential for microbial virulence and is critical for promoting the survival of Y. pestis in serum. Structures of Ail have been determined by X-ray diffraction and solution NMR spectroscopy, but the protein's activity is influenced by the detergents in these samples, underscoring the importance of the surrounding environment for structure-activity studies. Here we describe the backbone structure of Ail, determined in lipid bilayer nanodiscs, using solution NMR spectroscopy. We also present solid-state NMR data obtained for Ail in membranes containing lipopolysaccharide (LPS), a major component of the bacterial outer membranes. The protein in lipid bilayers, adopts the same eight-stranded β-barrel fold observed in the crystalline and micellar states. The membrane composition, however, appears to have a marked effect on protein dynamics, with LPS enhancing conformational order and slowing down the N transverse relaxation rate. The results provide information about the way in which an outer membrane protein inserts and functions in the bacterial membrane. PubMed: 28726410DOI: 10.1021/acs.jpcb.7b03941 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
