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

作者：Brillet Karl; Meksem Ahmed; Lauber Emmanuelle; Reimmann Cornelia; Cobessi David^*

来源：Acta Crystallographica Section D-Biological Crystallography, 2009, 65(4): 326-331.

DOI：10.1107/S0907444909002200

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 angstrom resolution is discussed.

• 出版日期2009-4
• 单位中国地震局