Role of Conformational Changes of Hexameric Bacterial Uridine Phosphorylases in Substrate Binding
Crystals of mutants of uridine phosphorylase from Shewanella oneidensis MR-1 at the active-site threonine residue were obtained, and the three-dimensional structures of the mutants were determined. It was shown that the loop 161–179 responsible for the nucleoside recognition is involved in stabiliza...
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| Veröffentlicht in: | Crystallography reports 2021-09, Vol.66 (5), p.786-790 |
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| container_title | Crystallography reports |
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| creator | Polyakov, K. M. Mordkovich, N. N. Safonova, T. N. Antipov, A. N. Okorokova, N. A. Dorovatovskii, P. V. Veiko, V. P. |
| description | Crystals of mutants of uridine phosphorylase from
Shewanella oneidensis
MR-1 at the active-site threonine residue were obtained, and the three-dimensional structures of the mutants were determined. It was shown that the loop 161–179 responsible for the nucleoside recognition is involved in stabilization of the hexameric structure of the protein and its disorder significantly facilitates the access of nucleoside to the enzyme active site. The role of conformational changes in the enzyme function is discussed. |
| doi_str_mv | 10.1134/S1063774521050199 |
| format | Article |
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Shewanella oneidensis
MR-1 at the active-site threonine residue were obtained, and the three-dimensional structures of the mutants were determined. It was shown that the loop 161–179 responsible for the nucleoside recognition is involved in stabilization of the hexameric structure of the protein and its disorder significantly facilitates the access of nucleoside to the enzyme active site. The role of conformational changes in the enzyme function is discussed.</description><identifier>ISSN: 1063-7745</identifier><identifier>EISSN: 1562-689X</identifier><identifier>DOI: 10.1134/S1063774521050199</identifier><language>eng</language><publisher>Moscow: Pleiades Publishing</publisher><subject>Crystallography and Scattering Methods ; Enzymes ; Nucleosides ; Phosphorylases ; Physics ; Physics and Astronomy ; Structure of Macromolecular Compounds ; Substrates</subject><ispartof>Crystallography reports, 2021-09, Vol.66 (5), p.786-790</ispartof><rights>Pleiades Publishing, Inc. 2021. ISSN 1063-7745, Crystallography Reports, 2021, Vol. 66, No. 5, pp. 786–790. © Pleiades Publishing, Inc., 2021. Russian Text © The Author(s), 2021, published in Kristallografiya, 2021, Vol. 66, No. 5, pp. 759–764.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c316t-36408dd982036120ec34998130c48832776bcf6889822e5c04fc187c0270cf413</citedby><cites>FETCH-LOGICAL-c316t-36408dd982036120ec34998130c48832776bcf6889822e5c04fc187c0270cf413</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1134/S1063774521050199$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1134/S1063774521050199$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids></links><search><creatorcontrib>Polyakov, K. M.</creatorcontrib><creatorcontrib>Mordkovich, N. N.</creatorcontrib><creatorcontrib>Safonova, T. N.</creatorcontrib><creatorcontrib>Antipov, A. N.</creatorcontrib><creatorcontrib>Okorokova, N. A.</creatorcontrib><creatorcontrib>Dorovatovskii, P. V.</creatorcontrib><creatorcontrib>Veiko, V. P.</creatorcontrib><title>Role of Conformational Changes of Hexameric Bacterial Uridine Phosphorylases in Substrate Binding</title><title>Crystallography reports</title><addtitle>Crystallogr. Rep</addtitle><description>Crystals of mutants of uridine phosphorylase from
Shewanella oneidensis
MR-1 at the active-site threonine residue were obtained, and the three-dimensional structures of the mutants were determined. It was shown that the loop 161–179 responsible for the nucleoside recognition is involved in stabilization of the hexameric structure of the protein and its disorder significantly facilitates the access of nucleoside to the enzyme active site. The role of conformational changes in the enzyme function is discussed.</description><subject>Crystallography and Scattering Methods</subject><subject>Enzymes</subject><subject>Nucleosides</subject><subject>Phosphorylases</subject><subject>Physics</subject><subject>Physics and Astronomy</subject><subject>Structure of Macromolecular Compounds</subject><subject>Substrates</subject><issn>1063-7745</issn><issn>1562-689X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><recordid>eNp1kEFLAzEUhIMoWKs_wNuC59X3kmw2OdpFrVBQrAVvS5om7ZbtpiZbsP_elAoexNMbmG8G3hByjXCLyPjdFEGwsuQFRSgAlTohAywEzYVUH6dJJzs_-OfkIsY1AEiJfED0m29t5l1W-c75sNF94zvdZtVKd0sbD87YfumNDY3JRtr0SSR7FppF09nsdeXjduXDvtUx0U2XTXfz2Afd22zUdIlZXpIzp9tor37ukMweH96rcT55eXqu7ie5YSj6nAkOcrFQkgITSMEaxpWSyMBwKRktSzE3TkiZCGoLA9wZlKUBWoJxHNmQ3Bx7t8F_7mzs67XfhfRLrGlRKqaK1JEoPFIm-BiDdfU2NBsd9jVCfViy_rNkytBjJiY2rRJ-m_8PfQPLVnP3</recordid><startdate>20210901</startdate><enddate>20210901</enddate><creator>Polyakov, K. M.</creator><creator>Mordkovich, N. N.</creator><creator>Safonova, T. N.</creator><creator>Antipov, A. N.</creator><creator>Okorokova, N. A.</creator><creator>Dorovatovskii, P. V.</creator><creator>Veiko, V. P.</creator><general>Pleiades Publishing</general><general>Springer Nature B.V</general><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>20210901</creationdate><title>Role of Conformational Changes of Hexameric Bacterial Uridine Phosphorylases in Substrate Binding</title><author>Polyakov, K. M. ; Mordkovich, N. N. ; Safonova, T. N. ; Antipov, A. N. ; Okorokova, N. A. ; Dorovatovskii, P. V. ; Veiko, V. P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c316t-36408dd982036120ec34998130c48832776bcf6889822e5c04fc187c0270cf413</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Crystallography and Scattering Methods</topic><topic>Enzymes</topic><topic>Nucleosides</topic><topic>Phosphorylases</topic><topic>Physics</topic><topic>Physics and Astronomy</topic><topic>Structure of Macromolecular Compounds</topic><topic>Substrates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Polyakov, K. M.</creatorcontrib><creatorcontrib>Mordkovich, N. N.</creatorcontrib><creatorcontrib>Safonova, T. N.</creatorcontrib><creatorcontrib>Antipov, A. N.</creatorcontrib><creatorcontrib>Okorokova, N. A.</creatorcontrib><creatorcontrib>Dorovatovskii, P. V.</creatorcontrib><creatorcontrib>Veiko, V. P.</creatorcontrib><collection>CrossRef</collection><jtitle>Crystallography reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Polyakov, K. M.</au><au>Mordkovich, N. N.</au><au>Safonova, T. N.</au><au>Antipov, A. N.</au><au>Okorokova, N. A.</au><au>Dorovatovskii, P. V.</au><au>Veiko, V. P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Role of Conformational Changes of Hexameric Bacterial Uridine Phosphorylases in Substrate Binding</atitle><jtitle>Crystallography reports</jtitle><stitle>Crystallogr. Rep</stitle><date>2021-09-01</date><risdate>2021</risdate><volume>66</volume><issue>5</issue><spage>786</spage><epage>790</epage><pages>786-790</pages><issn>1063-7745</issn><eissn>1562-689X</eissn><abstract>Crystals of mutants of uridine phosphorylase from
Shewanella oneidensis
MR-1 at the active-site threonine residue were obtained, and the three-dimensional structures of the mutants were determined. It was shown that the loop 161–179 responsible for the nucleoside recognition is involved in stabilization of the hexameric structure of the protein and its disorder significantly facilitates the access of nucleoside to the enzyme active site. The role of conformational changes in the enzyme function is discussed.</abstract><cop>Moscow</cop><pub>Pleiades Publishing</pub><doi>10.1134/S1063774521050199</doi><tpages>5</tpages></addata></record> |
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| subjects | Crystallography and Scattering Methods Enzymes Nucleosides Phosphorylases Physics Physics and Astronomy Structure of Macromolecular Compounds Substrates |
| title | Role of Conformational Changes of Hexameric Bacterial Uridine Phosphorylases in Substrate Binding |
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