Structure of the light‐driven sodium pump KR2 and its implications for optogenetics
A key and common process present in organisms from all domains of life is the maintenance of the ion gradient between the inside and the outside of the cell. The gradient is generated by various active transporters, among which are the light‐driven ion pumps of the microbial rhodopsin family. Wherea...
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| Veröffentlicht in: | The FEBS journal 2016-04, Vol.283 (7), p.1232-1238 |
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| description | A key and common process present in organisms from all domains of life is the maintenance of the ion gradient between the inside and the outside of the cell. The gradient is generated by various active transporters, among which are the light‐driven ion pumps of the microbial rhodopsin family. Whereas the proton‐pumping and anion‐pumping rhodopsins have been known for a long time, the cation (sodium) pumps were described only recently. Following the discovery, high‐resolution atomic structures of the pump KR2 were determined that revealed the complete ion translocation pathway, including the positions of the characteristic Asn‐Asp‐Gln (NDQ) triad, the unusual ion uptake cavity acting as a selectivity filter, the unique N‐terminal α‐helix, capping the ion release cavity, and unexpected flexibility of the retinal‐binding pocket. The structures also revealed pentamerization of KR2 and binding of sodium ions at the interface. Finally, on the basis of the structures, potassium‐pumping KR2 variants have been designed, making the findings even more important for optogenetic applications. In this Structural Snapshot, we analyse the implications of the structural findings for understanding the sodium translocation mechanism and application of the pump and its mutants in optogenetics.
Microbial rhodopsins (MRs) are a large family of photoactive membrane proteins. Recently, a new class of MRs, light‐driven sodium pumps have been discovered, and several atomic resolution structures have been determined. In this structural snapshot, we analyze and compare the structures, and discuss their implications for understanding the mechanism of light‐driven ion translocation. |
| doi_str_mv | 10.1111/febs.13585 |
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Microbial rhodopsins (MRs) are a large family of photoactive membrane proteins. Recently, a new class of MRs, light‐driven sodium pumps have been discovered, and several atomic resolution structures have been determined. In this structural snapshot, we analyze and compare the structures, and discuss their implications for understanding the mechanism of light‐driven ion translocation.</description><identifier>ISSN: 1742-464X</identifier><identifier>EISSN: 1742-4658</identifier><identifier>DOI: 10.1111/febs.13585</identifier><identifier>PMID: 26535564</identifier><language>eng</language><publisher>England: Blackwell Publishing Ltd</publisher><subject>Atomic structure ; Binding ; Binding Sites - genetics ; Biochemistry, Molecular Biology ; Capping ; Cations ; Cellular biology ; crystal structure ; Crystallography, X-Ray ; Flexibility ; Genetics ; High resolution ; Holes ; Information processing ; Ion pumps ; Ion Transport - radiation effects ; Ions ; Life Sciences ; Light ; Light effects ; light‐driven ; Maintenance ; microbial rhodopsins ; Microbiology ; Microorganisms ; Models, Chemical ; Models, Molecular ; Mutants ; Mutation ; Na+/K+-exchanging ATPase ; Optics ; optogenetics tools ; Photolysis - radiation effects ; Potassium ; potassium pump ; Protein Engineering - methods ; Protein Multimerization ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Pumping ; Pumps ; Retina ; Rhodopsin ; Selectivity ; Sodium ; Sodium - chemistry ; Sodium - metabolism ; sodium pump ; Sodium-Potassium-Exchanging ATPase - chemistry ; Sodium-Potassium-Exchanging ATPase - genetics ; Sodium-Potassium-Exchanging ATPase - metabolism ; Structural Biology ; Translocation</subject><ispartof>The FEBS journal, 2016-04, Vol.283 (7), p.1232-1238</ispartof><rights>2015 FEBS</rights><rights>2015 FEBS.</rights><rights>Copyright © 2016 Federation of European Biochemical Societies</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Ffebs.13585$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Ffebs.13585$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>230,314,780,784,885,1417,1433,27924,27925,45574,45575,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26535564$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.univ-grenoble-alpes.fr/hal-01235921$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Gushchin, Ivan</creatorcontrib><creatorcontrib>Shevchenko, Vitaly</creatorcontrib><creatorcontrib>Polovinkin, Vitaly</creatorcontrib><creatorcontrib>Borshchevskiy, Valentin</creatorcontrib><creatorcontrib>Buslaev, Pavel</creatorcontrib><creatorcontrib>Bamberg, Ernst</creatorcontrib><creatorcontrib>Gordeliy, Valentin</creatorcontrib><title>Structure of the light‐driven sodium pump KR2 and its implications for optogenetics</title><title>The FEBS journal</title><addtitle>FEBS J</addtitle><description>A key and common process present in organisms from all domains of life is the maintenance of the ion gradient between the inside and the outside of the cell. The gradient is generated by various active transporters, among which are the light‐driven ion pumps of the microbial rhodopsin family. Whereas the proton‐pumping and anion‐pumping rhodopsins have been known for a long time, the cation (sodium) pumps were described only recently. Following the discovery, high‐resolution atomic structures of the pump KR2 were determined that revealed the complete ion translocation pathway, including the positions of the characteristic Asn‐Asp‐Gln (NDQ) triad, the unusual ion uptake cavity acting as a selectivity filter, the unique N‐terminal α‐helix, capping the ion release cavity, and unexpected flexibility of the retinal‐binding pocket. The structures also revealed pentamerization of KR2 and binding of sodium ions at the interface. Finally, on the basis of the structures, potassium‐pumping KR2 variants have been designed, making the findings even more important for optogenetic applications. In this Structural Snapshot, we analyse the implications of the structural findings for understanding the sodium translocation mechanism and application of the pump and its mutants in optogenetics.
Microbial rhodopsins (MRs) are a large family of photoactive membrane proteins. Recently, a new class of MRs, light‐driven sodium pumps have been discovered, and several atomic resolution structures have been determined. In this structural snapshot, we analyze and compare the structures, and discuss their implications for understanding the mechanism of light‐driven ion translocation.</description><subject>Atomic structure</subject><subject>Binding</subject><subject>Binding Sites - genetics</subject><subject>Biochemistry, Molecular Biology</subject><subject>Capping</subject><subject>Cations</subject><subject>Cellular biology</subject><subject>crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>Flexibility</subject><subject>Genetics</subject><subject>High resolution</subject><subject>Holes</subject><subject>Information processing</subject><subject>Ion pumps</subject><subject>Ion Transport - radiation effects</subject><subject>Ions</subject><subject>Life Sciences</subject><subject>Light</subject><subject>Light effects</subject><subject>light‐driven</subject><subject>Maintenance</subject><subject>microbial rhodopsins</subject><subject>Microbiology</subject><subject>Microorganisms</subject><subject>Models, Chemical</subject><subject>Models, Molecular</subject><subject>Mutants</subject><subject>Mutation</subject><subject>Na+/K+-exchanging ATPase</subject><subject>Optics</subject><subject>optogenetics tools</subject><subject>Photolysis - radiation effects</subject><subject>Potassium</subject><subject>potassium pump</subject><subject>Protein Engineering - methods</subject><subject>Protein Multimerization</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>Pumping</subject><subject>Pumps</subject><subject>Retina</subject><subject>Rhodopsin</subject><subject>Selectivity</subject><subject>Sodium</subject><subject>Sodium - chemistry</subject><subject>Sodium - metabolism</subject><subject>sodium pump</subject><subject>Sodium-Potassium-Exchanging ATPase - chemistry</subject><subject>Sodium-Potassium-Exchanging ATPase - genetics</subject><subject>Sodium-Potassium-Exchanging ATPase - metabolism</subject><subject>Structural Biology</subject><subject>Translocation</subject><issn>1742-464X</issn><issn>1742-4658</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kc1OwzAMxyMEgjG48AAoEhc4dCRN0rTHMfElJiEBk7hFWZOyTG1TmnSIG4_AM_IkZGzswAHLki37J8v2H4AjjAY42Hmhp26ACUvZFuhhTuOIJizd3uT0eQ_sOzdHiDCaZbtgL04YYSyhPTB59G2X-67V0BbQzzQszcvMf318qtYsdA2dVaarYNNVDbx7iKGsFTTeQVM1pcmlN7Z2sLAttI23L7rW3uTuAOwUsnT6cB37YHJ1-TS6icb317ej4TiaUcpYRAgOKxWMcJ5imVOSUZ4liuucIqQU5UqrLOUcK0kKJuVUazlFEnGcckIKRfrgbDV3JkvRtKaS7buw0oib4VgsawjHhGUxXuDAnq7YprWvnXZeVMbluixlrW3nBOY8S9OY4SSgJ3_Que3aOlwicIaS4ITH_1JhVoLCs3mgjtdUN6202mz5K0EA8Ap4M6V-3_QxEktxxVJc8SOuuLq8ePzJyDeh7JWB</recordid><startdate>201604</startdate><enddate>201604</enddate><creator>Gushchin, Ivan</creator><creator>Shevchenko, Vitaly</creator><creator>Polovinkin, Vitaly</creator><creator>Borshchevskiy, Valentin</creator><creator>Buslaev, Pavel</creator><creator>Bamberg, Ernst</creator><creator>Gordeliy, Valentin</creator><general>Blackwell Publishing Ltd</general><general>Wiley</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>1XC</scope></search><sort><creationdate>201604</creationdate><title>Structure of the light‐driven sodium pump KR2 and its implications for optogenetics</title><author>Gushchin, Ivan ; 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The gradient is generated by various active transporters, among which are the light‐driven ion pumps of the microbial rhodopsin family. Whereas the proton‐pumping and anion‐pumping rhodopsins have been known for a long time, the cation (sodium) pumps were described only recently. Following the discovery, high‐resolution atomic structures of the pump KR2 were determined that revealed the complete ion translocation pathway, including the positions of the characteristic Asn‐Asp‐Gln (NDQ) triad, the unusual ion uptake cavity acting as a selectivity filter, the unique N‐terminal α‐helix, capping the ion release cavity, and unexpected flexibility of the retinal‐binding pocket. The structures also revealed pentamerization of KR2 and binding of sodium ions at the interface. Finally, on the basis of the structures, potassium‐pumping KR2 variants have been designed, making the findings even more important for optogenetic applications. In this Structural Snapshot, we analyse the implications of the structural findings for understanding the sodium translocation mechanism and application of the pump and its mutants in optogenetics.
Microbial rhodopsins (MRs) are a large family of photoactive membrane proteins. Recently, a new class of MRs, light‐driven sodium pumps have been discovered, and several atomic resolution structures have been determined. In this structural snapshot, we analyze and compare the structures, and discuss their implications for understanding the mechanism of light‐driven ion translocation.</abstract><cop>England</cop><pub>Blackwell Publishing Ltd</pub><pmid>26535564</pmid><doi>10.1111/febs.13585</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Atomic structure Binding Binding Sites - genetics Biochemistry, Molecular Biology Capping Cations Cellular biology crystal structure Crystallography, X-Ray Flexibility Genetics High resolution Holes Information processing Ion pumps Ion Transport - radiation effects Ions Life Sciences Light Light effects light‐driven Maintenance microbial rhodopsins Microbiology Microorganisms Models, Chemical Models, Molecular Mutants Mutation Na+/K+-exchanging ATPase Optics optogenetics tools Photolysis - radiation effects Potassium potassium pump Protein Engineering - methods Protein Multimerization Protein Structure, Secondary Protein Structure, Tertiary Pumping Pumps Retina Rhodopsin Selectivity Sodium Sodium - chemistry Sodium - metabolism sodium pump Sodium-Potassium-Exchanging ATPase - chemistry Sodium-Potassium-Exchanging ATPase - genetics Sodium-Potassium-Exchanging ATPase - metabolism Structural Biology Translocation |
| title | Structure of the light‐driven sodium pump KR2 and its implications for optogenetics |
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