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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Bibliographic Details
Published in:Biochemistry (Moscow) 2007-01, Vol.72 (1), p.93-99
Main Authors: Rodina, E V, Vorobyeva, N N, Kurilova, S A, Belenikin, M S, Fedorova, N V, Nazarova, T I
Format: Article
Language:English
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
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Summary: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.
ISSN:0006-2979
1608-3040
0320-9725
DOI:10.1134/S0006297907010117