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ATP as effector of inorganic pyrophosphatase of Escherichia coli. Identification of the binding site for ATP
The interaction of Escherichia coli inorganic pyrophosphatase (E-PPase) with effector ATP has been studied. The E-PPase has been chemically modified with the dialdehyde derivative of ATP. It has been established that in the experiment only one molecule of effector ATP is bound to each subunit of the...
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| Published in: | Biochemistry (Moscow) 2007-01, Vol.72 (1), p.93-99 |
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| Main Authors: | , , , , , |
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| container_end_page | 99 |
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| container_start_page | 93 |
| container_title | Biochemistry (Moscow) |
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| creator | Rodina, E V Vorobyeva, N N Kurilova, S A Belenikin, M S Fedorova, N V Nazarova, T I |
| description | The interaction of Escherichia coli inorganic pyrophosphatase (E-PPase) with effector ATP has been studied. The E-PPase has been chemically modified with the dialdehyde derivative of ATP. It has been established that in the experiment only one molecule of effector ATP is bound to each subunit of the hexameric enzyme. Tryptic digestion of the adenylated protein followed by isolation of a modified peptide by HPLC and its mass-spectrometric identification has showed that it is an amino group of Lys146 that undergoes modification. Molecular docking of ATP to E-PPase indicates that the binding site for effector ATP is located in a cluster of positively charged amino acid residues proposed earlier on the basis of site-directed mutagenesis to participate in binding of effector pyrophosphate. Molecular docking also reveals several other amino acid residues probably involved in the interaction with effectors. |
| doi_str_mv | 10.1134/S0006297907010117 |
| format | article |
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Identification of the binding site for ATP</title><source>Springer Link</source><creator>Rodina, E V ; Vorobyeva, N N ; Kurilova, S A ; Belenikin, M S ; Fedorova, N V ; Nazarova, T I</creator><creatorcontrib>Rodina, E V ; Vorobyeva, N N ; Kurilova, S A ; Belenikin, M S ; Fedorova, N V ; Nazarova, T I</creatorcontrib><description>The interaction of Escherichia coli inorganic pyrophosphatase (E-PPase) with effector ATP has been studied. The E-PPase has been chemically modified with the dialdehyde derivative of ATP. It has been established that in the experiment only one molecule of effector ATP is bound to each subunit of the hexameric enzyme. Tryptic digestion of the adenylated protein followed by isolation of a modified peptide by HPLC and its mass-spectrometric identification has showed that it is an amino group of Lys146 that undergoes modification. Molecular docking of ATP to E-PPase indicates that the binding site for effector ATP is located in a cluster of positively charged amino acid residues proposed earlier on the basis of site-directed mutagenesis to participate in binding of effector pyrophosphate. 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Identification of the binding site for ATP</title><title>Biochemistry (Moscow)</title><addtitle>Biochemistry (Mosc)</addtitle><description>The interaction of Escherichia coli inorganic pyrophosphatase (E-PPase) with effector ATP has been studied. The E-PPase has been chemically modified with the dialdehyde derivative of ATP. It has been established that in the experiment only one molecule of effector ATP is bound to each subunit of the hexameric enzyme. Tryptic digestion of the adenylated protein followed by isolation of a modified peptide by HPLC and its mass-spectrometric identification has showed that it is an amino group of Lys146 that undergoes modification. Molecular docking of ATP to E-PPase indicates that the binding site for effector ATP is located in a cluster of positively charged amino acid residues proposed earlier on the basis of site-directed mutagenesis to participate in binding of effector pyrophosphate. 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Identification of the binding site for ATP</atitle><jtitle>Biochemistry (Moscow)</jtitle><addtitle>Biochemistry (Mosc)</addtitle><date>2007-01</date><risdate>2007</risdate><volume>72</volume><issue>1</issue><spage>93</spage><epage>99</epage><pages>93-99</pages><issn>0006-2979</issn><eissn>1608-3040</eissn><eissn>0320-9725</eissn><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>The interaction of Escherichia coli inorganic pyrophosphatase (E-PPase) with effector ATP has been studied. The E-PPase has been chemically modified with the dialdehyde derivative of ATP. It has been established that in the experiment only one molecule of effector ATP is bound to each subunit of the hexameric enzyme. Tryptic digestion of the adenylated protein followed by isolation of a modified peptide by HPLC and its mass-spectrometric identification has showed that it is an amino group of Lys146 that undergoes modification. Molecular docking of ATP to E-PPase indicates that the binding site for effector ATP is located in a cluster of positively charged amino acid residues proposed earlier on the basis of site-directed mutagenesis to participate in binding of effector pyrophosphate. Molecular docking also reveals several other amino acid residues probably involved in the interaction with effectors.</abstract><cop>United States</cop><pub>Springer Nature B.V</pub><pmid>17309442</pmid><doi>10.1134/S0006297907010117</doi><tpages>7</tpages></addata></record> |
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| ispartof | Biochemistry (Moscow), 2007-01, Vol.72 (1), p.93-99 |
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| subjects | Adenosine Triphosphate - chemistry Adenosine Triphosphate - metabolism Amino acids Binding Sites Biochemistry Diphosphates - metabolism Dose-Response Relationship, Drug E coli Enzymes Escherichia coli Escherichia coli - enzymology Inorganic Pyrophosphatase - chemistry Inorganic Pyrophosphatase - metabolism Magnesium Compounds - metabolism Models, Molecular Molecular biology Molecular Structure Protein Structure, Quaternary Protein Structure, Tertiary Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Structure-Activity Relationship |
| title | ATP as effector of inorganic pyrophosphatase of Escherichia coli. Identification of the binding site for ATP |
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