1. Molecular strategies to replace the structural metal site in the prokaryotic zinc finger domain
- Author
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Alessia Rivellino, Luigi Russo, Ilaria Baglivo, Maddalena Palmieri, Rosa Iacovino, Carla Isernia, Paolo V. Pedone, Sabrina Esposito, Fortuna Netti, Biancamaria Farina, Roberto Fattorusso, Gaetano Malgieri, Baglivo, I, Palmieri, M, Rivellino, A, Netti, F, Russo, Luigi, Esposito, Sabrina, Iacovino, Rosa, Farina, B, Isernia, Carla, Fattorusso, Roberto, Pedone, Paolo Vincenzo, and Malgieri, Gaetano more...
- 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 - 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. more...
- Published
- 2014
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