3EFM

Structure of the alcaligin outer membrane recepteur FauA from Bordetella pertussis

Summary for 3EFM

• Entry DOI: 10.2210/pdb3efm/pdb
• Descriptor: Ferric alcaligin siderophore receptor, SULFATE ION (3 entities in total)
• Functional Keywords: membrane protein, membrane receptor, membrane transporter, siderophore, membrane, receptor, tonb box
• Biological source: Bordetella pertussis
• Cellular location: Cell outer membrane (By similarity): Q9X6A5
• Total number of polymer chains: 1
• Total formula weight: 78869.97

Authors

Brillet, K.,Lauber, E.,Reimmann, C.,Armstrong, S.K.,Cobessi, D. (deposition date: 2008-09-09, release date: 2009-03-31, Last modification date: 2023-11-01)

Primary citation

Brillet, K.,Meksem, A.,Lauber, E.,Reimmann, C.,Cobessi, D.
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 Crystallogr.,Sect.D, 65:326-331, 2009

PubMed Abstract: 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.

PubMed: 19307713
DOI: 10.1107/S0907444909002200

Experimental method

X-RAY DIFFRACTION (2.33 Å)