A TonB-dependent outer membrane protein as aBacteroides fragilisfibronectin-binding molecule
نویسندگان
چکیده
منابع مشابه
Mechanics of force propagation in TonB-dependent outer membrane transport.
For the uptake of scarce yet essential organometallic compounds, outer membrane transporters of Gram-negative bacteria work in concert with an energy-generating inner membrane complex, thus spanning the periplasmic space to drive active transport. Here, we examine the interaction of TonB, an inner membrane protein, with an outer membrane transporter based upon a recent crystal structure of a To...
متن کاملReconstitution of bacterial outer membrane TonB-dependent transporters in planar lipid bilayer membranes.
Micronutrients such as siderophore-bound iron and vitamin B(12) cross the outer membrane of gram-negative bacteria through a group of 22-stranded beta-barrel proteins. They share the unusual feature that their N-terminal end inserts from the periplasmic side into the beta-barrel and plugs the lumen. Transport results from energy-driven movement of TonB protein, which either pulls the plug out o...
متن کاملStudy of the immunogenicity of outer membrane protein A (ompA) gene from Acinetobacter baumannii as DNA vaccine candidate in vivo
Objective(s): Acinetobacter baumannii is one the most dangerous opportunistic pathogens in hospitalized infections. This bacterium is resistant to 90% of commercial antibiotics. Therefore, developing new strategies to cure A. baumannii-infections is urgent. The DNA vaccines new approach in which the immunogen can be directly expressed inside the target cells through cl...
متن کاملEnhanced binding of TonB to a ligand-loaded outer membrane receptor: role of the oligomeric state of TonB in formation of a functional FhuA.TonB complex.
The ferric hydroxymate uptake (FhuA) receptor from Escherichia coli facilitates transport of siderophores ferricrocin and ferrichrome and siderophore-antibiotic conjugates such as albomycin and rifamycin CGP 4832. FhuA is also the receptor for phages T5, T1, Phi80, UC-1, for colicin M and for the antimicrobial peptide microcin MccJ21. Energy for transport is provided by the cytoplasmic membrane...
متن کاملCompeting ligands stabilize alternate conformations of the energy coupling motif of a TonB-dependent outer membrane transporter.
BtuB is a TonB-dependent outer-membrane transporter for vitamin B12 (or cyanocobalamin, CN-Cbl) in Escherichia coli. The binding of CN-Cbl is believed to promote an unfolding or undocking of the Ton box, the conserved N-terminal energy coupling motif at the periplasmic surface of the transporter. This structural change may facilitate the interaction of BtuB with the inner membrane protein TonB....
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: FEMS Immunology & Medical Microbiology
سال: 2009
ISSN: 0928-8244,1574-695X
DOI: 10.1111/j.1574-695x.2009.00532.x