Three-dimensional structure of thymidine phosphorylase from Escherichia coli at 2.8 A resolution
The three-dimensional structure of thymidine phosphorylase from Escherichia coli has been determined at 2.8 A resolution using multiple-isomorphous-replacement techniques. The amino acid sequence deduced from the deoA DNA sequence is also reported. Thymidine phosphorylase exists in the crystal as an...
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| Veröffentlicht in: | The Journal of biological chemistry 1990-08, Vol.265 (23), p.14016-14022 |
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| container_end_page | 14022 |
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| container_issue | 23 |
| container_start_page | 14016 |
| container_title | The Journal of biological chemistry |
| container_volume | 265 |
| creator | Walter, M R Cook, W J Cole, L B Short, S A Koszalka, G W Krenitsky, T A Ealick, S E |
| description | The three-dimensional structure of thymidine phosphorylase from Escherichia coli has been determined at 2.8 A resolution using
multiple-isomorphous-replacement techniques. The amino acid sequence deduced from the deoA DNA sequence is also reported.
Thymidine phosphorylase exists in the crystal as an S-shaped dimer in which the subunits are related by a crystallographic
2-fold axis. Each subunit is composed of a small alpha-helical domain of six helices and a large alpha/beta domain. The alpha/beta
domain includes a six-stranded mixed beta-sheet and a four-stranded antiparallel beta-sheet. The active site has been identified
by difference Fourier analyses of the binding of thymine and thymidine and lies in a cavity between the small and large domains.
The central beta-sheet is splayed open to accommodate a putative phosphate-binding site which is probably occupied by a sulfate
ion in the crystal. |
| doi_str_mv | 10.1016/s0021-9258(18)77450-4 |
| format | Article |
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multiple-isomorphous-replacement techniques. The amino acid sequence deduced from the deoA DNA sequence is also reported.
Thymidine phosphorylase exists in the crystal as an S-shaped dimer in which the subunits are related by a crystallographic
2-fold axis. Each subunit is composed of a small alpha-helical domain of six helices and a large alpha/beta domain. The alpha/beta
domain includes a six-stranded mixed beta-sheet and a four-stranded antiparallel beta-sheet. The active site has been identified
by difference Fourier analyses of the binding of thymine and thymidine and lies in a cavity between the small and large domains.
The central beta-sheet is splayed open to accommodate a putative phosphate-binding site which is probably occupied by a sulfate
ion in the crystal.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/s0021-9258(18)77450-4</identifier><identifier>PMID: 2199449</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Binding Sites ; Cloning, Molecular ; Crystallization ; DNA, Bacterial - genetics ; Escherichia coli - enzymology ; Ligands ; Models, Molecular ; Molecular Sequence Data ; Pentosyltransferases - genetics ; Pentosyltransferases - isolation & purification ; Protein Conformation ; Thymidine Phosphorylase - genetics ; Thymidine Phosphorylase - isolation & purification ; X-Ray Diffraction</subject><ispartof>The Journal of biological chemistry, 1990-08, Vol.265 (23), p.14016-14022</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3614-370ad06d2c98c542a46519d1fb968eb73a8a22ab055c9322f37f0b62dbdd9bb63</citedby><cites>FETCH-LOGICAL-c3614-370ad06d2c98c542a46519d1fb968eb73a8a22ab055c9322f37f0b62dbdd9bb63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,778,782,27911,27912</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2199449$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Walter, M R</creatorcontrib><creatorcontrib>Cook, W J</creatorcontrib><creatorcontrib>Cole, L B</creatorcontrib><creatorcontrib>Short, S A</creatorcontrib><creatorcontrib>Koszalka, G W</creatorcontrib><creatorcontrib>Krenitsky, T A</creatorcontrib><creatorcontrib>Ealick, S E</creatorcontrib><title>Three-dimensional structure of thymidine phosphorylase from Escherichia coli at 2.8 A resolution</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The three-dimensional structure of thymidine phosphorylase from Escherichia coli has been determined at 2.8 A resolution using
multiple-isomorphous-replacement techniques. The amino acid sequence deduced from the deoA DNA sequence is also reported.
Thymidine phosphorylase exists in the crystal as an S-shaped dimer in which the subunits are related by a crystallographic
2-fold axis. Each subunit is composed of a small alpha-helical domain of six helices and a large alpha/beta domain. The alpha/beta
domain includes a six-stranded mixed beta-sheet and a four-stranded antiparallel beta-sheet. The active site has been identified
by difference Fourier analyses of the binding of thymine and thymidine and lies in a cavity between the small and large domains.
The central beta-sheet is splayed open to accommodate a putative phosphate-binding site which is probably occupied by a sulfate
ion in the crystal.</description><subject>Amino Acid Sequence</subject><subject>Binding Sites</subject><subject>Cloning, Molecular</subject><subject>Crystallization</subject><subject>DNA, Bacterial - genetics</subject><subject>Escherichia coli - enzymology</subject><subject>Ligands</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Pentosyltransferases - genetics</subject><subject>Pentosyltransferases - isolation & purification</subject><subject>Protein Conformation</subject><subject>Thymidine Phosphorylase - genetics</subject><subject>Thymidine Phosphorylase - isolation & purification</subject><subject>X-Ray Diffraction</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kElLxDAUx4MoOi4fQchBRA_VvCxtc5TBDQQPKniL2Woj7WRMWmS-vR1n8MHjHf7Lgx9Cp0CugEB5nQmhUEgq6guoL6uKC1LwHTQDUrOCCXjfRbN_ywE6zPmLTMMl7KN9ClJyLmfo47VN3hcu9H6RQ1zoDuchjXYYk8exwUO76oMLC4-XbczTplWns8dNij2-zbb1Kdg2aGxjF7AeML2q8Q1OPsduHKbCY7TX6C77k-09Qm93t6_zh-Lp-f5xfvNUWFYCL1hFtCOlo1bWVnCqeSlAOmiMLGtvKqZrTak2RAgrGaUNqxpiSuqMc9KYkh2h803vMsXv0edB9SFb33V64eOYVSUlJRxgMoqN0aaYc_KNWqbQ67RSQNSarHpZY1NrbApq9UdW8Sl3un0wmt67_9QW5aSfbfQ2fLY_IXllQpz49IqWQlGmgE_l7BfwI4C8</recordid><startdate>19900815</startdate><enddate>19900815</enddate><creator>Walter, M R</creator><creator>Cook, W J</creator><creator>Cole, L B</creator><creator>Short, S A</creator><creator>Koszalka, G W</creator><creator>Krenitsky, T A</creator><creator>Ealick, S E</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19900815</creationdate><title>Three-dimensional structure of thymidine phosphorylase from Escherichia coli at 2.8 A resolution</title><author>Walter, M R ; Cook, W J ; Cole, L B ; Short, S A ; Koszalka, G W ; Krenitsky, T A ; Ealick, S E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3614-370ad06d2c98c542a46519d1fb968eb73a8a22ab055c9322f37f0b62dbdd9bb63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Amino Acid Sequence</topic><topic>Binding Sites</topic><topic>Cloning, Molecular</topic><topic>Crystallization</topic><topic>DNA, Bacterial - genetics</topic><topic>Escherichia coli - enzymology</topic><topic>Ligands</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Pentosyltransferases - genetics</topic><topic>Pentosyltransferases - isolation & purification</topic><topic>Protein Conformation</topic><topic>Thymidine Phosphorylase - genetics</topic><topic>Thymidine Phosphorylase - isolation & purification</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Walter, M R</creatorcontrib><creatorcontrib>Cook, W J</creatorcontrib><creatorcontrib>Cole, L B</creatorcontrib><creatorcontrib>Short, S A</creatorcontrib><creatorcontrib>Koszalka, G W</creatorcontrib><creatorcontrib>Krenitsky, T A</creatorcontrib><creatorcontrib>Ealick, S E</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Walter, M R</au><au>Cook, W J</au><au>Cole, L B</au><au>Short, S A</au><au>Koszalka, G W</au><au>Krenitsky, T A</au><au>Ealick, S E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Three-dimensional structure of thymidine phosphorylase from Escherichia coli at 2.8 A resolution</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1990-08-15</date><risdate>1990</risdate><volume>265</volume><issue>23</issue><spage>14016</spage><epage>14022</epage><pages>14016-14022</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The three-dimensional structure of thymidine phosphorylase from Escherichia coli has been determined at 2.8 A resolution using
multiple-isomorphous-replacement techniques. The amino acid sequence deduced from the deoA DNA sequence is also reported.
Thymidine phosphorylase exists in the crystal as an S-shaped dimer in which the subunits are related by a crystallographic
2-fold axis. Each subunit is composed of a small alpha-helical domain of six helices and a large alpha/beta domain. The alpha/beta
domain includes a six-stranded mixed beta-sheet and a four-stranded antiparallel beta-sheet. The active site has been identified
by difference Fourier analyses of the binding of thymine and thymidine and lies in a cavity between the small and large domains.
The central beta-sheet is splayed open to accommodate a putative phosphate-binding site which is probably occupied by a sulfate
ion in the crystal.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>2199449</pmid><doi>10.1016/s0021-9258(18)77450-4</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1990-08, Vol.265 (23), p.14016-14022 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Binding Sites Cloning, Molecular Crystallization DNA, Bacterial - genetics Escherichia coli - enzymology Ligands Models, Molecular Molecular Sequence Data Pentosyltransferases - genetics Pentosyltransferases - isolation & purification Protein Conformation Thymidine Phosphorylase - genetics Thymidine Phosphorylase - isolation & purification X-Ray Diffraction |
| title | Three-dimensional structure of thymidine phosphorylase from Escherichia coli at 2.8 A resolution |
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