Differences between CusA and AcrB crystallisation highlighted by protein flexibility.
BACKGROUND
Until very recently, AcrB was the only Resistance Nodulation and cell Division transporter for which the structure has been elucidated. Towards a general understanding of this protein family, CusA and AcrB were compared.


RESULTS
In dodecylmaltoside, AcrB crystallised in many different conditions, while CusA does not. This could be due to the difference in dynamic between these proteins as judged from limited proteolysis assays. Addition of various compounds, in particular heavy metal cations, stabilises CusA.


CONCLUSIONS
This approach could constitute a first step towards CusA crystallisation.
Deniaud
Aurélien
A
Institut de Biologie Structurale Jean Pierre Ebel, UMR5075 CEA-CNRS-Université Joseph Fourier, Grenoble, France.
Goulielmakis
Aurélie
A
Covès
Jacques
J
Pebay-Peyroula
Eva
E
D000595:Amino Acid Sequence; D002413:Cations, Divalent; D003460:Crystallization; D029968:Escherichia coli Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D027425:ATP-Binding Cassette, Sub-Family C Proteins / Q000737:chemistry*; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
D002413:Cations, Divalent; D029968:Escherichia coli Proteins; D027425:ATP-Binding Cassette, Sub-Family C Proteins; C083496:AcrB protein, E coli