Article: article from journal or magazin.
Use of an in-house approach to study the three-dimensional structures of various outer membrane proteins: structure of the alcaligin outer membrane transporter FauA from Bordetella pertussis.
Acta Crystallographica. Section D, Biological Crystallography
Bordetella pertussis is the bacterial agent of whooping cough in humans. Under iron-limiting conditions, it produces the siderophore alcaligin. Released to the extracellular environment, alcaligin chelates iron, which is then taken up as a ferric alcaligin complex via the FauA outer membrane transporter. FauA belongs to a family of TonB-dependent outer membrane transporters that function using energy derived from the proton motive force. Using an in-house protocol for membrane-protein expression, purification and crystallization, FauA was crystallized in its apo form together with three other TonB-dependent transporters from different organisms. Here, the protocol used to study FauA is described and its three-dimensional structure determined at 2.3 A resolution is discussed.
Apoproteins/chemistry, Bacterial Outer Membrane Proteins/chemistry, Bacterial Outer Membrane Proteins/isolation & purification, Bacterial Proteins/metabolism, Bordetella pertussis/chemistry, Crystallography, X-Ray, Hydroxamic Acids/metabolism, Iron/metabolism, Membrane Proteins/metabolism, Models, Molecular, Protein Conformation, Protein Interaction Mapping, Protons, Receptors, Cell Surface/chemistry, Receptors, Cell Surface/isolation & purification, Recombinant Fusion Proteins/chemistry, Recombinant Fusion Proteins/isolation & purification
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