Structural changes in the recombinant, NADP(H)-binding component of proton translocating transhydrogenase revealed by NMR spectroscopy
We have analysed 1H, 15N-HSQC spectra of the recombinant, NADP(H)-binding component of transhydrogenase in the context of the emerging three dimensional structure of the protein. Chemical shift perturbations of amino acid residues following replacement of NADP + with NADPH were observed in both the...
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| Veröffentlicht in: | FEBS letters 1999-03, Vol.446 (1), p.127-132 |
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| creator | Quirk, Philip G. Jeeves, Mark Cotton, Nick P.J. Smith, John K. Jackson, Baz J. |
| description | We have analysed
1H,
15N-HSQC spectra of the recombinant, NADP(H)-binding component of transhydrogenase in the context of the emerging three dimensional structure of the protein. Chemical shift perturbations of amino acid residues following replacement of NADP
+ with NADPH were observed in both the adenosine and nicotinamide parts of the dinucleotide binding site and in a region which straddles the protein. These observations reflect the structural changes resulting from hydride transfer. The interactions between the recombinant, NADP(H)-binding component and its partner, NAD(H)-binding protein, are complicated. Helix B of the recombinant, NADP(H)-binding component may play an important role in the binding process. |
| doi_str_mv | 10.1016/S0014-5793(99)00198-2 |
| format | Article |
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1H,
15N-HSQC spectra of the recombinant, NADP(H)-binding component of transhydrogenase in the context of the emerging three dimensional structure of the protein. Chemical shift perturbations of amino acid residues following replacement of NADP
+ with NADPH were observed in both the adenosine and nicotinamide parts of the dinucleotide binding site and in a region which straddles the protein. These observations reflect the structural changes resulting from hydride transfer. The interactions between the recombinant, NADP(H)-binding component and its partner, NAD(H)-binding protein, are complicated. Helix B of the recombinant, NADP(H)-binding component may play an important role in the binding process.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(99)00198-2</identifier><identifier>PMID: 10100628</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Binding Sites ; Escherichia coli - metabolism ; Magnetic Resonance Spectroscopy ; Model structure ; Molecular Sequence Data ; NADP - metabolism ; NADP Transhydrogenases - chemistry ; NADP Transhydrogenases - metabolism ; Nicotinamide nucleotide ; NMR ; Recombinant Proteins - chemistry ; Recombinant Proteins - metabolism ; Rhodospirillum rubrum ; Transhydrogenase</subject><ispartof>FEBS letters, 1999-03, Vol.446 (1), p.127-132</ispartof><rights>1999 Federation of European Biochemical Societies</rights><rights>FEBS Letters 446 (1999) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5252-ec35b6b6740b94b019428d75b9a304b12df5827000e3d7d943b811739ba7e63c3</citedby><cites>FETCH-LOGICAL-c5252-ec35b6b6740b94b019428d75b9a304b12df5827000e3d7d943b811739ba7e63c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2899%2900198-2$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0014-5793(99)00198-2$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,777,781,1412,1428,3537,27905,27906,45555,45556,45976,46390,46814</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10100628$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Quirk, Philip G.</creatorcontrib><creatorcontrib>Jeeves, Mark</creatorcontrib><creatorcontrib>Cotton, Nick P.J.</creatorcontrib><creatorcontrib>Smith, John K.</creatorcontrib><creatorcontrib>Jackson, Baz J.</creatorcontrib><title>Structural changes in the recombinant, NADP(H)-binding component of proton translocating transhydrogenase revealed by NMR spectroscopy</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>We have analysed
1H,
15N-HSQC spectra of the recombinant, NADP(H)-binding component of transhydrogenase in the context of the emerging three dimensional structure of the protein. Chemical shift perturbations of amino acid residues following replacement of NADP
+ with NADPH were observed in both the adenosine and nicotinamide parts of the dinucleotide binding site and in a region which straddles the protein. These observations reflect the structural changes resulting from hydride transfer. The interactions between the recombinant, NADP(H)-binding component and its partner, NAD(H)-binding protein, are complicated. Helix B of the recombinant, NADP(H)-binding component may play an important role in the binding process.</description><subject>Amino Acid Sequence</subject><subject>Binding Sites</subject><subject>Escherichia coli - metabolism</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Model structure</subject><subject>Molecular Sequence Data</subject><subject>NADP - metabolism</subject><subject>NADP Transhydrogenases - chemistry</subject><subject>NADP Transhydrogenases - metabolism</subject><subject>Nicotinamide nucleotide</subject><subject>NMR</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - metabolism</subject><subject>Rhodospirillum rubrum</subject><subject>Transhydrogenase</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNUctu1DAUtRCIDoVPAHmFWomAHeflVVVKyyCVgiisLT_uzBhl7GB7ivIDfDdOUiF2sLKOz7nnPg5Czyl5TQlt3twSQquibjk74fw0A94V5QO0ol3LClY13UO0-iM5Qk9i_E4y7ih_jI6yAyFN2a3Qr9sUDjodguyx3km3hYitw2kHOID2e2WddOkVvjl_9_lkfVpkbKzb4kwN3oFL2G_wEHzyuShIF3uvZZoUM9qNJvgtOBknvzuQPRisRnzz8QuOA-gUfNR-GJ-iRxvZR3h2_x6jb1eXXy_WxfWn9x8uzq8LXZd1WYBmtWpU01ZE8UrlpauyM22tuGSkUrQ0m7or27woMNMaXjHVUdoyrmQLDdPsGL1cfPPIPw4Qk9jbqKHvpQN_iKLhTd02rMrCehHqPGEMsBFDsHsZRkGJmAIQcwBiuq7gXMwBiDLXvbhvcFB7MH9VLRfPgvUi-Gl7GP_PVVxdvi1nZiI4n7-nXmeLFeSL3VkIImoLToOxObskjLf_mPY3rPiqww</recordid><startdate>19990305</startdate><enddate>19990305</enddate><creator>Quirk, Philip G.</creator><creator>Jeeves, Mark</creator><creator>Cotton, Nick P.J.</creator><creator>Smith, John K.</creator><creator>Jackson, Baz J.</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><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>19990305</creationdate><title>Structural changes in the recombinant, NADP(H)-binding component of proton translocating transhydrogenase revealed by NMR spectroscopy</title><author>Quirk, Philip G. ; Jeeves, Mark ; Cotton, Nick P.J. ; Smith, John K. ; Jackson, Baz J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5252-ec35b6b6740b94b019428d75b9a304b12df5827000e3d7d943b811739ba7e63c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Amino Acid Sequence</topic><topic>Binding Sites</topic><topic>Escherichia coli - metabolism</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Model structure</topic><topic>Molecular Sequence Data</topic><topic>NADP - metabolism</topic><topic>NADP Transhydrogenases - chemistry</topic><topic>NADP Transhydrogenases - metabolism</topic><topic>Nicotinamide nucleotide</topic><topic>NMR</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - metabolism</topic><topic>Rhodospirillum rubrum</topic><topic>Transhydrogenase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Quirk, Philip G.</creatorcontrib><creatorcontrib>Jeeves, Mark</creatorcontrib><creatorcontrib>Cotton, Nick P.J.</creatorcontrib><creatorcontrib>Smith, John K.</creatorcontrib><creatorcontrib>Jackson, Baz J.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Quirk, Philip G.</au><au>Jeeves, Mark</au><au>Cotton, Nick P.J.</au><au>Smith, John K.</au><au>Jackson, Baz J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural changes in the recombinant, NADP(H)-binding component of proton translocating transhydrogenase revealed by NMR spectroscopy</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1999-03-05</date><risdate>1999</risdate><volume>446</volume><issue>1</issue><spage>127</spage><epage>132</epage><pages>127-132</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>We have analysed
1H,
15N-HSQC spectra of the recombinant, NADP(H)-binding component of transhydrogenase in the context of the emerging three dimensional structure of the protein. Chemical shift perturbations of amino acid residues following replacement of NADP
+ with NADPH were observed in both the adenosine and nicotinamide parts of the dinucleotide binding site and in a region which straddles the protein. These observations reflect the structural changes resulting from hydride transfer. The interactions between the recombinant, NADP(H)-binding component and its partner, NAD(H)-binding protein, are complicated. Helix B of the recombinant, NADP(H)-binding component may play an important role in the binding process.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>10100628</pmid><doi>10.1016/S0014-5793(99)00198-2</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 1999-03, Vol.446 (1), p.127-132 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_69657634 |
| source | MEDLINE; Wiley Online Library; Elsevier ScienceDirect Journals; Wiley-Blackwell Full Collection; Alma/SFX Local Collection; EZB Electronic Journals Library |
| subjects | Amino Acid Sequence Binding Sites Escherichia coli - metabolism Magnetic Resonance Spectroscopy Model structure Molecular Sequence Data NADP - metabolism NADP Transhydrogenases - chemistry NADP Transhydrogenases - metabolism Nicotinamide nucleotide NMR Recombinant Proteins - chemistry Recombinant Proteins - metabolism Rhodospirillum rubrum Transhydrogenase |
| title | Structural changes in the recombinant, NADP(H)-binding component of proton translocating transhydrogenase revealed by NMR spectroscopy |
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