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.


Autoria(s): Brillet K.; Meksem A.; Lauber E.; Reimmann C.; Cobessi D.
Data(s)

2009

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