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.
Data(s) |
2009
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Resumo |
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. |
Identificador |
http://serval.unil.ch/?id=serval:BIB_5869DA0DD92E isbn:1399-0047[electronic], 0907-4449[linking] pmid:19307713 doi:10.1107/S0907444909002200 isiid:000264361500003 |
Idioma(s) |
en |
Fonte |
Acta Crystallographica. Section D, Biological Crystallography, vol. 65, no. Pt 4, pp. 326-331 |
Palavras-Chave | #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 |
Tipo |
info:eu-repo/semantics/article article |