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.
Détails
ID Serval
serval:BIB_5869DA0DD92E
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
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.
Périodique
Acta Crystallographica. Section D, Biological Crystallography
ISSN
1399-0047[electronic], 0907-4449[linking]
Statut éditorial
Publié
Date de publication
2009
Peer-reviewed
Oui
Volume
65
Numéro
Pt 4
Pages
326-331
Langue
anglais
Résumé
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.
Mots-clé
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
Pubmed
Web of science
Création de la notice
02/02/2010 16:33
Dernière modification de la notice
20/08/2019 15:12