1H, 15N and 13C resonance assignment of the periplasmic domain of outer membrane protein A from Acinetobacter baumannii

Abstract

Acinetobacter baumannii is a multiple drug resistant pathogen that causes pneumonia, bacteremia, wound infections and urinary tract infections in immunocompromised patients. Outer membrane protein A of Acinetobacter baumannii (AbOmpA) is a major surface protein and induces host cell death. AbOmpA is supposed to be composed of N-terminal β-barrel transmembrane domain and C-terminal periplasmic domain. The periplasmic domain of AbOmpA forms an OmpA-like fold, which is involved in the non-covalent interaction with peptidoglycan. However, its three dimensional structure is not determined yet. Here, we report the cloning, expression, purification and NMR spectroscopy study of recombinant AbOmpA periplasmic domain (AbOmpA-PD). The NMR spectrum of AbOmpA-PD is well dispered and almost signals exhibit homogeneous, which allow us to assign the backbone signals thoroughly. This study provides a clue for structural study of AbOmpA-PD.

Keywords

• OmpA-like fold
• OmpA
• Backbone assignment
• NMR