3EPV

X-ray Structure of the Metal-sensor CnrX in both the Apo- and Copper-bound Forms

Summary for 3EPV

• Entry DOI: 10.2210/pdb3epv/pdb
• Descriptor: Nickel and cobalt resistance protein cnrR, COPPER (II) ION (3 entities in total)
• Functional Keywords: all alpha helix, cobalt, nickel, metal binding protein
• Biological source: Ralstonia metallidurans
• Cellular location: Periplasm: P37975
• Total number of polymer chains: 4
• Total formula weight: 49829.87

Authors

Pompidor, G.,Maillard, A.P.,Girard, E.,Gambarelli, S.,Kahn, R.,Coves, J. (deposition date: 2008-09-30, release date: 2008-11-25, Last modification date: 2024-10-30)

Primary citation

Pompidor, G.,Maillard, A.P.,Girard, E.,Gambarelli, S.,Kahn, R.,Coves, J.
X-ray structure of the metal-sensor CnrX in both the apo- and copper-bound forms.
Febs Lett., 2008

PubMed Abstract: 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.

PubMed: 18992246
DOI: 10.1016/j.febslet.2008.10.042

Experimental method

X-RAY DIFFRACTION (1.742 Å)