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Molecular strategies to replace the structural metal site in the prokaryotic zinc finger domain
Molecular strategies to replace the structural metal site in the prokaryotic zinc finger domain
- Source :
- Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1844:497-504
- Publication Year :
- 2014
- Publisher :
- Elsevier BV, 2014.
-
Abstract
- The specific arrangement of secondary elements in a local motif often totally relies on the formation of coordination bonds between metal ions and protein ligands. This is typified by the -30 amino acid eukaryotic zinc finger motif in which a beta-sheet and an or-helix are clustered around a zinc ion by various combinations of four ligands. The prokaryotic zinc finger domain (found in the Ros protein from Agrobacterium tumefaciens) is different from the eukaryotic counterpart as it consists of 58 amino acids arranged in a beta beta beta alpha alpha topology stabilized by a 15-residue hydrophobic core. Also, this domain tetrahedrally coordinates zinc and unfolds in the absence of the metal ion.The characterization of proteins belonging to the Ros homologs family has however shown that the prokaryotic zinc finger domain can overcome the metal requirement to achieve the same fold and DNA-binding activity. In the present work, two zinc-lacking Ros homologs (MI4 and MI5 proteins) have been thoroughly characterized using bioinformatics, biochemical and NMR techniques.We show how in these proteins a network of hydrogen bonds and hydrophobic interactions surrogate the zinc coordination role in the achievement of the same functional fold.(c) 2013 Published by Elsevier B.V.
- Subjects :
- Models, Molecular
Molecular Sequence Data
Biophysics
chemistry.chemical_element
Electrophoretic Mobility Shift Assay
Zinc
Biology
Biochemistry
Analytical Chemistry
Bacterial Proteins
Amino Acid Sequence
DNA binding
Nuclear Magnetic Resonance, Biomolecular
Molecular Biology
LIM domain
Prokaryotic zinc finger
Zinc finger
chemistry.chemical_classification
Thermal unfolding
Sequence Homology, Amino Acid
Circular Dichroism
Zinc Fingers
DNA
Zinc finger nuclease
Amino acid
RING finger domain
Crystallography
chemistry
Agrobacterium tumefaciens
Metals
PHD finger
Mutation
Protein ligand
Subjects
Details
- ISSN :
- 15709639
- Volume :
- 1844
- Database :
- OpenAIRE
- Journal :
- Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- Accession number :
- edsair.doi.dedup.....4d61342651838a4a3371f3d8b1f82072
- Full Text :
- https://doi.org/10.1016/j.bbapap.2013.12.019