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Comparison of Spatial Structures and Packaging of Phosphorybosil Pyrophosphate Synthetase 2 from Thermus thermophilus HB27 in Rhombohedral and Tetragonal Crystals

Autor: Yulia Abramchik, Evgeniy Zayats, Maria Kostromina, Dmitry Lykoshin, Ilya Fateev, Irina Konstantinova, Nadezda Zhukhlistova, Vladimir Timofeev, Inna Kuranova, Roman Esipov

Publikováno v: Crystals, Vol 11, Iss 9, p 1128 (2021)

We report the spatial structure of phosphoribosyl pyrophosphate synthetase 2 from the thermophilic bacterium Thermus thermophilus HB27 (TthPRPPS2) obtained at a 1.85 Å resolution using a diffraction set collected from rhombohedral crystals (space gr

Externí odkaz: https://doaj.org/article/f62e568b2fdf4309ab75b50993c7b399

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Comparison of Spatial Structures and Packaging of Phosphorybosil Pyrophosphate Synthetase 2 from Thermus thermophilus HB27 in Rhombohedral and Tetragonal Crystals

Autor: Roman S. Esipov, Vladimir I. Timofeev, Yulia Abramchik, Nadezda Zhukhlistova, Irina D. Konstantinova, D. D. Lykoshin, Evgeniy A Zayats, M. A. Kostromina, Ilya Fateev, Inna P. Kuranova

Publikováno v: Crystals, Vol 11, Iss 1128, p 1128 (2021)
Crystals
Volume 11
Issue 9

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f7c0c4441cdbf2ee8c47b2016e41029
https://www.mdpi.com/2073-4352/11/9/1128

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Crystal structure of Escherichia coli purine nucleoside phosphorylase in complex with 7-deazahypoxanthine

Autor: M. A. Kostromina, Ilya Fateev, Y.A. Abramchik, N. E. Zhukhlistova, Roman S. Esipov, Inna P. Kuranova, Vladimir I. Timofeev, T. I. Muravieva

Publikováno v: Acta Crystallogr F Struct Biol Commun

Purine nucleoside phosphorylases (EC 2.4.2.1; PNPs) reversibly catalyze the phosphorolytic cleavage of glycosidic bonds in purine nucleosides to generate ribose 1-phosphate and a free purine base, and are key enzymes in the salvage pathway of purine

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7c28e9ea0ec6decc2cd705800beb984
https://pubmed.ncbi.nlm.nih.gov/29870020

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3'-Azidothymidine in the active site of Escherichia coli thymidine phosphorylase: the peculiarity of the binding on the basis of X-ray study

Autor: Nadezda Zhukhlistova, T. I. Muravieva, Vladimir I. Timofeev, Roman S. Esipov, Yulia Abramchik, Ilya Fateev, Inna P. Kuranova

Publikováno v: Acta crystallographica. Section D, Biological crystallography. 70(Pt 4)

The structural study of complexes of thymidine phosphorylase (TP) with nucleoside analogues which inhibit its activity is of special interest because many of these compounds are used as chemotherapeutic agents. Determination of kinetic parameters sho

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b907fc7cb704d7423e5cb5c75f580d37
https://pubmed.ncbi.nlm.nih.gov/24699659

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