Structural Characterization of a Putative Endogenous Metal Chelator in the Periplasmic Nickel Transporter NikA
Escherichia coli and related bacteria require nickel for the synthesis of hydrogenases, enzymes involved in hydrogen oxidation and proton reduction. Nickel transport to the cytoplasm depends on five proteins, NikA−E. We have previously reported the three-dimensional structure of the soluble periplas...
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| Veröffentlicht in: | Biochemistry (Easton) 2008-09, Vol.47 (38), p.9937-9943 |
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| container_issue | 38 |
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| container_title | Biochemistry (Easton) |
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| creator | Cherrier, Mickaël V Cavazza, Christine Bochot, Constance Lemaire, David Fontecilla-Camps, Juan C |
| description | Escherichia coli and related bacteria require nickel for the synthesis of hydrogenases, enzymes involved in hydrogen oxidation and proton reduction. Nickel transport to the cytoplasm depends on five proteins, NikA−E. We have previously reported the three-dimensional structure of the soluble periplasmic nickel transporter NikA in a complex with FeEDTA(H2O)−. We have now determined the structure of EDTA-free NikA and have found that it binds a small organic molecule that contributes three ligands to the coordination of a transition metal ion. Unexpectedly, His416, which was far from the metal-binding site in the FeEDTA(H2O)−−NikA complex, becomes the fourth observed ligand to the metal. The best match to the omit map electron density is obtained for butane-1,2,4-tricarboxylate (BTC). Our attempts to obtain a BTC−Ni−NikA complex using apo protein and commercial reagents resulted in nickel-free BTC−NikA. Overall, our results suggest that nickel transport in vivo requires a specific metallophore that may be BTC. |
| doi_str_mv | 10.1021/bi801051y |
| format | Article |
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Nickel transport to the cytoplasm depends on five proteins, NikA−E. We have previously reported the three-dimensional structure of the soluble periplasmic nickel transporter NikA in a complex with FeEDTA(H2O)−. We have now determined the structure of EDTA-free NikA and have found that it binds a small organic molecule that contributes three ligands to the coordination of a transition metal ion. Unexpectedly, His416, which was far from the metal-binding site in the FeEDTA(H2O)−−NikA complex, becomes the fourth observed ligand to the metal. The best match to the omit map electron density is obtained for butane-1,2,4-tricarboxylate (BTC). Our attempts to obtain a BTC−Ni−NikA complex using apo protein and commercial reagents resulted in nickel-free BTC−NikA. Overall, our results suggest that nickel transport in vivo requires a specific metallophore that may be BTC.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi801051y</identifier><identifier>PMID: 18759453</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>ATP-Binding Cassette Transporters - chemistry ; Chelating Agents - chemistry ; Chelating Agents - metabolism ; Crystallography, X-Ray ; Escherichia coli Proteins - chemistry ; Escherichia coli Proteins - metabolism ; Nickel - metabolism ; Periplasm - metabolism ; Protein Structure, Secondary - physiology</subject><ispartof>Biochemistry (Easton), 2008-09, Vol.47 (38), p.9937-9943</ispartof><rights>Copyright © 2008 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a417t-904cb5067562529203e380ad0dd1c5667e169b2effe5d2be3398212ca7bc8eb73</citedby><cites>FETCH-LOGICAL-a417t-904cb5067562529203e380ad0dd1c5667e169b2effe5d2be3398212ca7bc8eb73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi801051y$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi801051y$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18759453$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cherrier, Mickaël V</creatorcontrib><creatorcontrib>Cavazza, Christine</creatorcontrib><creatorcontrib>Bochot, Constance</creatorcontrib><creatorcontrib>Lemaire, David</creatorcontrib><creatorcontrib>Fontecilla-Camps, Juan C</creatorcontrib><title>Structural Characterization of a Putative Endogenous Metal Chelator in the Periplasmic Nickel Transporter NikA</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>Escherichia coli and related bacteria require nickel for the synthesis of hydrogenases, enzymes involved in hydrogen oxidation and proton reduction. Nickel transport to the cytoplasm depends on five proteins, NikA−E. We have previously reported the three-dimensional structure of the soluble periplasmic nickel transporter NikA in a complex with FeEDTA(H2O)−. We have now determined the structure of EDTA-free NikA and have found that it binds a small organic molecule that contributes three ligands to the coordination of a transition metal ion. Unexpectedly, His416, which was far from the metal-binding site in the FeEDTA(H2O)−−NikA complex, becomes the fourth observed ligand to the metal. The best match to the omit map electron density is obtained for butane-1,2,4-tricarboxylate (BTC). Our attempts to obtain a BTC−Ni−NikA complex using apo protein and commercial reagents resulted in nickel-free BTC−NikA. Overall, our results suggest that nickel transport in vivo requires a specific metallophore that may be BTC.</description><subject>ATP-Binding Cassette Transporters - chemistry</subject><subject>Chelating Agents - chemistry</subject><subject>Chelating Agents - metabolism</subject><subject>Crystallography, X-Ray</subject><subject>Escherichia coli Proteins - chemistry</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Nickel - metabolism</subject><subject>Periplasm - metabolism</subject><subject>Protein Structure, Secondary - physiology</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkE9v1DAQxS0EotvCgS-AfAGph8DYie34WFblj9QuK3WRuFmOM6HuZuPFdhDl02PYVblwGr2Z37zRPEJeMHjDgLO3nW-BgWD3j8iCCQ5Vo7V4TBYAICuuJZyQ05TuimxANU_JCWuV0I2oF2S6yXF2eY52pMtbG63LGP0vm32YaBiopes5F_UD6eXUh284hTnRa8x_eRxtDpH6ieZbpOuyuR9t2nlHV95tcaSbaKe0D7GYltb24hl5Mtgx4fNjPSNf3l9ulh-rq88fPi0vrirbMJUrDY3rBEglJBdcc6ixbsH20PfMCSkVMqk7jsOAoucd1rVuOePOqs612Kn6jLw--O5j-D5jymbnk8NxtBOWB4zUorzfQAHPD6CLIaWIg9lHv7Px3jAwf8I1D-EW9uXRdO522P8jj2kWoDoAPmX8-TC3cWukqpUwm_WNuV59XQr5bmXWhX914K1L5i7McSqZ_Ofwb95ukMQ</recordid><startdate>20080923</startdate><enddate>20080923</enddate><creator>Cherrier, Mickaël V</creator><creator>Cavazza, Christine</creator><creator>Bochot, Constance</creator><creator>Lemaire, David</creator><creator>Fontecilla-Camps, Juan C</creator><general>American Chemical Society</general><scope>BSCLL</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>20080923</creationdate><title>Structural Characterization of a Putative Endogenous Metal Chelator in the Periplasmic Nickel Transporter NikA</title><author>Cherrier, Mickaël V ; Cavazza, Christine ; Bochot, Constance ; Lemaire, David ; Fontecilla-Camps, Juan C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a417t-904cb5067562529203e380ad0dd1c5667e169b2effe5d2be3398212ca7bc8eb73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>ATP-Binding Cassette Transporters - chemistry</topic><topic>Chelating Agents - chemistry</topic><topic>Chelating Agents - metabolism</topic><topic>Crystallography, X-Ray</topic><topic>Escherichia coli Proteins - chemistry</topic><topic>Escherichia coli Proteins - metabolism</topic><topic>Nickel - metabolism</topic><topic>Periplasm - metabolism</topic><topic>Protein Structure, Secondary - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cherrier, Mickaël V</creatorcontrib><creatorcontrib>Cavazza, Christine</creatorcontrib><creatorcontrib>Bochot, Constance</creatorcontrib><creatorcontrib>Lemaire, David</creatorcontrib><creatorcontrib>Fontecilla-Camps, Juan C</creatorcontrib><collection>Istex</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>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cherrier, Mickaël V</au><au>Cavazza, Christine</au><au>Bochot, Constance</au><au>Lemaire, David</au><au>Fontecilla-Camps, Juan C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural Characterization of a Putative Endogenous Metal Chelator in the Periplasmic Nickel Transporter NikA</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>2008-09-23</date><risdate>2008</risdate><volume>47</volume><issue>38</issue><spage>9937</spage><epage>9943</epage><pages>9937-9943</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>Escherichia coli and related bacteria require nickel for the synthesis of hydrogenases, enzymes involved in hydrogen oxidation and proton reduction. Nickel transport to the cytoplasm depends on five proteins, NikA−E. We have previously reported the three-dimensional structure of the soluble periplasmic nickel transporter NikA in a complex with FeEDTA(H2O)−. We have now determined the structure of EDTA-free NikA and have found that it binds a small organic molecule that contributes three ligands to the coordination of a transition metal ion. Unexpectedly, His416, which was far from the metal-binding site in the FeEDTA(H2O)−−NikA complex, becomes the fourth observed ligand to the metal. The best match to the omit map electron density is obtained for butane-1,2,4-tricarboxylate (BTC). Our attempts to obtain a BTC−Ni−NikA complex using apo protein and commercial reagents resulted in nickel-free BTC−NikA. Overall, our results suggest that nickel transport in vivo requires a specific metallophore that may be BTC.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>18759453</pmid><doi>10.1021/bi801051y</doi><tpages>7</tpages></addata></record> |
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| subjects | ATP-Binding Cassette Transporters - chemistry Chelating Agents - chemistry Chelating Agents - metabolism Crystallography, X-Ray Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism Nickel - metabolism Periplasm - metabolism Protein Structure, Secondary - physiology |
| title | Structural Characterization of a Putative Endogenous Metal Chelator in the Periplasmic Nickel Transporter NikA |
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