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- Title
Biostructural analysis of the metal-sensor domain of CnrX from Cupriavidus metallidurans CH34.
- Authors
Guillaume Pompidor; Eric Girard; Antoine Maillard; Stéphanie Ramella-Pairin; Beate Bersch; Richard Kahn; Jacques Covès
- Abstract
Abstract In Cupriavidus metallidurans CH34, the proteins CnrX, CnrY, and CnrH regulate the expression of the cnrCBA operon that codes for a cation-efflux pump involved in cobalt and nickel resistance. The periplasmic part of CnrX can be defined as the metal sensor in the signal transduction complex composed of the membrane-bound anti-sigma factor CnrY and the extra-cytoplasmic function sigma factor CnrH. A soluble form of CnrX was overproduced and purified. This protein behaves as a dimer in solution as judged from gel filtration, sedimentation velocity experiments, and NMR. Native crystals diffracting to 2.3 Å using synchrotron radiation were obtained using the hanging-drop vapor-diffusion method. They belong to the primitive monoclinic space group P21, with unit cell parameters a = 31.87, b = 74.80, c = 93.67 Å, β = 90.107°. NMR data and secondary structure prediction suggest that this protein is essentially formed by helices.
- Subjects
STRUCTURAL analysis (Science); BACILLUS (Bacteria); BIOSENSORS; PROTEIN structure; EFFECT of metals on microorganisms; BACTERIAL proteins; OPERONS; COBALT -- Physiological effect; NICKEL; NUCLEAR magnetic resonance
- Publication
Antonie van Leeuwenhoek, 2009, Vol 96, Issue 2, p141
- ISSN
0003-6072
- Publication type
Article
- DOI
10.1007/s10482-008-9283-6