Zahran M, Berezniak T, Imhof P, Smith JC (2011)
Publication Type: Journal article
Publication year: 2011
Book Volume: 585
Pages Range: 2739-2743
Journal Issue: 17
DOI: 10.1016/j.febslet.2011.07.036
The restriction endonuclease EcoRV binds two magnesium ions. One of these ions, MgA2+, binds to the phosphate group where the cleavage occurs and is required for catalysis, but the role of the other ion, MgB2+ is debated. Here, multiple independent molecular dynamics simulations suggest that MgB2+ is crucial for achieving a tightly bound protein-DNA complex and stabilizing a conformation that allows cleavage. In the absence of MgB2+ in all simulations the protein-DNA hydrogen bond network is significantly disrupted and the sharp kink at the central base pair step of the DNA, which is observed in the two-metal complex, is not present. Also, the active site residues rearrange in such a way that the formation of a nucleophile, required for DNA hydrolysis, is unlikely. © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
APA:
Zahran, M., Berezniak, T., Imhof, P., & Smith, J.C. (2011). Role of magnesium ions in DNA recognition by the EcoRV restriction endonuclease. FEBS letters, 585(17), 2739-2743. https://dx.doi.org/10.1016/j.febslet.2011.07.036
MLA:
Zahran, Mai, et al. "Role of magnesium ions in DNA recognition by the EcoRV restriction endonuclease." FEBS letters 585.17 (2011): 2739-2743.
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