1H, 15N and 13C resonance assignment of the periplasmic domain of outer membrane protein A from Acinetobacter baumannii
| Autor: | Jeong Soon Park, Kyoung-Seok Ryu, Eunha Hwang, Chung-Kyung Lee, Young Ho Jeon, Hye-Yeon Kim |
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| Jazyk: | angličtina |
| Rok vydání: | 2010 |
| Předmět: | |
| Zdroj: | Journal of Analytical Science and Technology, Vol 1, Iss 2, Pp 113-117 (2010) |
| Druh dokumentu: | article |
| ISSN: | 2093-3134 2093-3371 |
| Popis: | 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. |
| Databáze: | Directory of Open Access Journals |
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