Publication Abstract from PubMed
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.
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.,Brillet K, Meksem A, Lauber E, Reimmann C, Cobessi D Acta Crystallogr D Biol Crystallogr. 2009 Apr;65(Pt 4):326-31. Epub 2009 Mar 19. PMID:19307713[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
