Faculty Collaboration Database

Structural Insights into the Yersinia pestis Outer Membrane Protein Ail in Lipid Bilayers. J Phys Chem B 2017 Aug 17;121(32):7561-7570

Date

07/21/2017

Pubmed ID

28726410

Pubmed Central ID

PMC5713880

DOI

10.1021/acs.jpcb.7b03941

Scopus ID

2-s2.0-85030760401 (requires institutional sign-in at Scopus site)   24 Citations

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 ¹⁵N transverse relaxation rate. The results provide information about the way in which an outer membrane protein inserts and functions in the bacterial membrane.

Author List

Dutta SK, Yao Y, Marassi FM

Author

Francesca M. Marassi PhD Chair, Professor in the Biophysics department at Medical College of Wisconsin

MESH terms used to index this publication - Major topics in bold

Amino Acid Sequence
Bacterial Outer Membrane Proteins
Calorimetry, Differential Scanning
Lipid Bilayers
Nanostructures
Nuclear Magnetic Resonance, Biomolecular
Protein Structure, Tertiary
Virulence Factors
X-Ray Diffraction
Yersinia pestis