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Structural and metal binding characterization of the C-terminal metallochaperone domain of membrane fusion protein SilB from Cupriavidus metallidurans CH34.
- Source :
-
Biochemistry [Biochemistry] 2011 Mar 29; Vol. 50 (12), pp. 2194-204. Date of Electronic Publication: 2011 Feb 22. - Publication Year :
- 2011
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Abstract
- Detoxification of heavy metal ions in Proteobacteria is tightly controlled by various systems regulating their sequestration and transport. In Cupriavidus metallidurans CH34, a model organism for heavy metal resistance studies, the sil determinant is potentially involved in the efflux of silver and copper ions. Proteins SilA, SilB, and SilC form a resistance nodulation cell division (RND)-based transport system in which SilB is the periplasmic adaptor protein belonging to the membrane fusion protein (MFP) family. In addition to the four domains typical of known MFPs, SilB has a fifth additional C-terminal domain, called SilB(440-521), which is characterized here. Structure and backbone dynamics of SilB(440-521) have been investigated using nuclear magnetic resonance, and the residues of the metal site were identified from (15)N- and (13)C-edited HSQC spectra. The solution structure and additional metal binding experiments demonstrated that this C-terminal domain folds independently of the rest of the protein and has a conformation and a Ag(+) and Cu(+) binding specificity similar to those determined for CusF from Escherichia coli. The small protein CusF plays a role in metal trafficking in the periplasm. The similarity with CusF suggests a potential metallochaperone role for SilB(440-521) that is discussed in the context of simultaneous expression of different determinants involved in copper resistance in C. metallidurans CH34.
- Subjects :
- Amino Acid Sequence
Bacterial Proteins chemistry
Bacterial Proteins isolation & purification
Bacterial Proteins metabolism
Binding Sites
Copper metabolism
Membrane Fusion Proteins isolation & purification
Metallochaperones isolation & purification
Models, Molecular
Molecular Sequence Data
Nuclear Magnetic Resonance, Biomolecular
Peptide Fragments chemistry
Peptide Fragments metabolism
Protein Binding
Protein Structure, Tertiary
Sequence Alignment
Silver metabolism
Substrate Specificity
Cupriavidus
Membrane Fusion Proteins chemistry
Membrane Fusion Proteins metabolism
Metallochaperones chemistry
Metallochaperones metabolism
Metals metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1520-4995
- Volume :
- 50
- Issue :
- 12
- Database :
- MEDLINE
- Journal :
- Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 21299248
- Full Text :
- https://doi.org/10.1021/bi200005k