Modeling of Phosphoribosylpyrophosphate Synthetase from Thermus Thermophilus in Complex with ATP and Ribose 5-Phosphate

Autor:	M.A. Kostromina, K. V. Sinitsyna, R. S. Esipov, A. A. Litunov, Vladimir I. Timofeev, T. I. Muravieva, Inna P. Kuranova, D. D. Podshivalov, D. D. Sidorov-Biryukov
Rok vydání:	2019
Předmět:	010302 applied physics chemistry.chemical_classification biology Stereochemistry Mutagenesis Active site General Chemistry Thermus thermophilus 010403 inorganic & nuclear chemistry Condensed Matter Physics biology.organism_classification 01 natural sciences Phosphoribosylpyrophosphate synthetase 0104 chemical sciences chemistry.chemical_compound Molecular dynamics Enzyme chemistry Ribose 5-phosphate 0103 physical sciences Ribose biology.protein General Materials Science
Zdroj:	Crystallography Reports. 64:94-97
ISSN:	1562-689X 1063-7745
DOI:	10.1134/s1063774519010206
Popis:	The positions of the substrates (ATP and ribose 5 phosphate) of phosphoribosylpyrophosphate synthetase from Thermus thermophilus were determined by molecular dynamics simulations. The simulation brought the system to an equilibrium state, with the binding poses of the ligands in the active site being stable. Based on the results of simulation of the complex, the environment of the substrates was analyzed and the amino-acid residues of the enzyme that form polar interactions with the substrates were identified. Candidate sites for mutagenesis, which can be mutated in order to broaden the substrate specificity toward ribose 5-phosphate, are proposed.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::8a208acefd99fd637b6733939c1c3b12 https://doi.org/10.1134/s1063774519010206 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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