X-ray structure of the metal-sensor CnrX in both the apo- and copper-bound forms.
Both the X-ray structures of the apo- and the copper-bound forms of the metal-sensor domain (residues 31-148) of CnrX from Cupriavidus metallidurans CH34 were obtained at 1.74A resolution from a selenomethionine derivative. This four-helix hooked-hairpin is the first structure of a metal-sensor in an ECF-type signaling pathway. The copper ion is bound in a type 2-like center with a 3N1O coordination in the equatorial plane and shows an unprecedented remote fifth axial ligand with Met93 contributing a weak S-Cu bond. The signal onset cannot be explained by conformational changes associated with CnrX metallation.
Pompidor
Guillaume
G
Laboratoire des Protéines Membranaires, Institut de Biologie Structurale - Jean-Pierre Ebel, UMR 5075 CNRS-CEA-UJF, 41, rue Jules Horowitz, 38027 Grenoble Cedex, France.
Maillard
Antoine P
AP
Girard
Eric
E
Gambarelli
Serge
S
Kahn
Richard
R
Covès
Jacques
J
D000595:Amino Acid Sequence; D001059:Apoproteins / Q000737:chemistry* / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D003300:Copper / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D049921:Cupriavidus / Q000378:metabolism*; D019281:Dimerization; D008969:Molecular Sequence Data; D033903:Periplasmic Proteins / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D017434:Protein Structure, Tertiary
D001059:Apoproteins; D001426:Bacterial Proteins; D033903:Periplasmic Proteins; D003300:Copper