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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

Authors :
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
Malgieri, Gaetano
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.

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