Structural aspects of catalytic mechanisms of endonucleases and their binding to nucleic acids
Identifieur interne : 002731 ( Istex/Corpus ); précédent : 002730; suivant : 002732Structural aspects of catalytic mechanisms of endonucleases and their binding to nucleic acids
Auteurs : N. E. Zhukhlistova ; V. V. Balaev ; A. V. Lyashenko ; A. A. LashkovSource :
- Crystallography Reports [ 1063-7745 ] ; 2012-05-01.
Abstract
Abstract: Endonucleases (EC 3.1) are enzymes of the hydrolase class that catalyze the hydrolytic cleavage of deoxyribonucleic and ribonucleic acids at any region of the polynucleotide chain. Endonucleases are widely used both in biotechnological processes and in veterinary medicine as antiviral agents. Medical applications of endonucleases in human cancer therapy hold promise. The results of X-ray diffraction studies of the spatial organization of endonucleases and their complexes and the mechanism of their action are analyzed and generalized. An analysis of the structural studies of this class of enzymes showed that the specific binding of enzymes to nucleic acids is characterized by interactions with nitrogen bases and the nucleotide backbone, whereas the nonspecific binding of enzymes is generally characterized by interactions only with the nucleic-acid backbone. It should be taken into account that the specificity can be modulated by metal ions and certain low-molecular-weight organic compounds. To test the hypotheses about specific and nonspecific nucleic-acid-binding proteins, it is necessary to perform additional studies of atomic-resolution three-dimensional structures of enzyme-nucleic-acid complexes by methods of structural biology.
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DOI: 10.1134/S1063774512030236
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Endonucleases are widely used both in biotechnological processes and in veterinary medicine as antiviral agents. Medical applications of endonucleases in human cancer therapy hold promise. The results of X-ray diffraction studies of the spatial organization of endonucleases and their complexes and the mechanism of their action are analyzed and generalized. An analysis of the structural studies of this class of enzymes showed that the specific binding of enzymes to nucleic acids is characterized by interactions with nitrogen bases and the nucleotide backbone, whereas the nonspecific binding of enzymes is generally characterized by interactions only with the nucleic-acid backbone. It should be taken into account that the specificity can be modulated by metal ions and certain low-molecular-weight organic compounds. To test the hypotheses about specific and nonspecific nucleic-acid-binding proteins, it is necessary to perform additional studies of atomic-resolution three-dimensional structures of enzyme-nucleic-acid complexes by methods of structural biology.</div></front></TEI><istex><corpusName>springer-journals</corpusName><author><json:item><name>N. E. Zhukhlistova</name><affiliations><json:string>Shubnikov Institute of Crystallography, Russian Academy of Sciences, Leninskii pr. 59, 119333, Moscow, Russia</json:string></affiliations></json:item><json:item><name>V. V. Balaev</name><affiliations><json:string>Shubnikov Institute of Crystallography, Russian Academy of Sciences, Leninskii pr. 59, 119333, Moscow, Russia</json:string></affiliations></json:item><json:item><name>A. V. Lyashenko</name><affiliations><json:string>Shubnikov Institute of Crystallography, Russian Academy of Sciences, Leninskii pr. 59, 119333, Moscow, Russia</json:string></affiliations></json:item><json:item><name>A. A. 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The results of X-ray diffraction studies of the spatial organization of endonucleases and their complexes and the mechanism of their action are analyzed and generalized. An analysis of the structural studies of this class of enzymes showed that the specific binding of enzymes to nucleic acids is characterized by interactions with nitrogen bases and the nucleotide backbone, whereas the nonspecific binding of enzymes is generally characterized by interactions only with the nucleic-acid backbone. It should be taken into account that the specificity can be modulated by metal ions and certain low-molecular-weight organic compounds. 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Endonucleases are widely used both in biotechnological processes and in veterinary medicine as antiviral agents. Medical applications of endonucleases in human cancer therapy hold promise. The results of X-ray diffraction studies of the spatial organization of endonucleases and their complexes and the mechanism of their action are analyzed and generalized. An analysis of the structural studies of this class of enzymes showed that the specific binding of enzymes to nucleic acids is characterized by interactions with nitrogen bases and the nucleotide backbone, whereas the nonspecific binding of enzymes is generally characterized by interactions only with the nucleic-acid backbone. It should be taken into account that the specificity can be modulated by metal ions and certain low-molecular-weight organic compounds. To test the hypotheses about specific and nonspecific nucleic-acid-binding proteins, it is necessary to perform additional studies of atomic-resolution three-dimensional structures of enzyme-nucleic-acid complexes by methods of structural biology.</Para></Abstract><ArticleNote Type="Misc"><SimplePara>Original Russian Text © N.E. Zhukhlistova, V.V. Balaev, A.V. Lyashenko, A.A. Lashkov, 2012, published in Kristallografiya, 2012, Vol. 57, No. 3, pp. 390–414.</SimplePara></ArticleNote><ArticleNote Type="Dedication"><SimplePara>Dedicated to the memory of A.V. 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Endonucleases are widely used both in biotechnological processes and in veterinary medicine as antiviral agents. Medical applications of endonucleases in human cancer therapy hold promise. The results of X-ray diffraction studies of the spatial organization of endonucleases and their complexes and the mechanism of their action are analyzed and generalized. An analysis of the structural studies of this class of enzymes showed that the specific binding of enzymes to nucleic acids is characterized by interactions with nitrogen bases and the nucleotide backbone, whereas the nonspecific binding of enzymes is generally characterized by interactions only with the nucleic-acid backbone. It should be taken into account that the specificity can be modulated by metal ions and certain low-molecular-weight organic compounds. 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|clé= ISTEX:D52183CD85F1A1F8B013721C7D90CBEEBE289693
|texte= Structural aspects of catalytic mechanisms of endonucleases and their binding to nucleic acids
}}
| This area was generated with Dilib version V0.6.33. |  |