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X-ray structure of the metal-sensor CnrX in both the apo- and copper-bound forms
- Source :
- FEBS Letters, FEBS Letters, 2008, 582 (28), pp.3954-3958. ⟨10.1016/j.febslet.2008.10.042⟩, FEBS Letters, Wiley, 2008, 582 (28), pp.3954-3958. ⟨10.1016/j.febslet.2008.10.042⟩
- Publication Year :
- 2008
-
Abstract
- International audience; 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.
- Subjects :
- Metal-sensor
Protein Conformation
[SDV]Life Sciences [q-bio]
MESH: Amino Acid Sequence
Signal transduction
Crystallography, X-Ray
01 natural sciences
Biochemistry
chemistry.chemical_compound
MESH: Apoproteins
MESH: Protein Structure, Tertiary
Protein structure
MESH: Protein Conformation
Structural Biology
Cupriavidus metallidurans CH34
MESH: Bacterial Proteins
0303 health sciences
biology
Resolution (electron density)
Cupriavidus
3. Good health
MESH: Copper
visual_art
visual_art.visual_art_medium
Periplasmic Proteins
Dimerization
Stereochemistry
Molecular Sequence Data
Biophysics
chemistry.chemical_element
CnrX
010402 general chemistry
Metal
03 medical and health sciences
Bacterial Proteins
Genetics
Amino Acid Sequence
Molecular Biology
030304 developmental biology
MESH: Cupriavidus
MESH: Molecular Sequence Data
Cupriavidus metallidurans
Ligand
Cell Biology
biology.organism_classification
MESH: Crystallography, X-Ray
Copper
0104 chemical sciences
Protein Structure, Tertiary
Crystallography
chemistry
MESH: Dimerization
X-ray structure
Apoproteins
Derivative (chemistry)
Heavy-metal
MESH: Periplasmic Proteins
Subjects
Details
- ISSN :
- 00145793 and 18733468
- Volume :
- 582
- Issue :
- 28
- Database :
- OpenAIRE
- Journal :
- FEBS letters
- Accession number :
- edsair.doi.dedup.....b24f8c368e60f2051ff9e93561de43ca
- Full Text :
- https://doi.org/10.1016/j.febslet.2008.10.042⟩