title: Differences between CusA and AcrB crystallisation highlighted by protein flexibility.
abstract: 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.
authors: Institut de Biologie Structurale Jean Pierre Ebel, UMR5075 CEA-CNRS-Université Joseph Fourier, Grenoble, France.
authors: Aurélien
authors: A
authors: Deniaud
authors: Aurélie
authors: A
authors: Goulielmakis
authors: Jacques
authors: J
authors: Covès
authors: Eva
authors: E
authors: Pebay-Peyroula
mesh_terms: 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
chemical_list: D002413:Cations, Divalent; D029968:Escherichia coli Proteins; D027425:ATP-Binding Cassette, Sub-Family C Proteins; C083496:AcrB protein, E coli