Identification of Asp804 and Asp808 as Na+ and K+ coordinating residues in α‐subunit of renal Na,K‐ATPase
Mutations to Asp804 and Asp808 in the α‐subunit almost abolish Na,K‐ATPase activity, but high‐affinity binding of [3H]ATP or [3H]ouabain at equilibrium and E1–E2 transitions are preserved. Titration of K+‐ion displacement of [3H]ATP or [3H]ouabain shows that the mutations interfere with occlusion of...
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| Veröffentlicht in: | FEBS letters 1997-01, Vol.400 (2), p.206-210 |
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| container_title | FEBS letters |
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| creator | Pedersen, Per Amstrup Rasmussen, Jakob H Nielsen, Jesper M Jorgensen, Peter L |
| description | Mutations to Asp804 and Asp808 in the α‐subunit almost abolish Na,K‐ATPase activity, but high‐affinity binding of [3H]ATP or [3H]ouabain at equilibrium and E1–E2 transitions are preserved. Titration of K+‐ion displacement of [3H]ATP or [3H]ouabain shows that the mutations interfere with occlusion of K+ in the E2[2K] conformation. Reduced phosphorylation levels or affinities for Na+ in presence of oligomycin indicate that Asp804 and Asp808 also contribute to coordination of Na+ in the E1P[3Na] form. Demonstration of alternate interactions of Na+ or K+ with Asp804 and Asp808 support the notion of cation binding in a ping‐pong sequence in catalytic models of Na,K‐pumping. |
| doi_str_mv | 10.1016/S0014-5793(96)01381-6 |
| format | Article |
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Titration of K+‐ion displacement of [3H]ATP or [3H]ouabain shows that the mutations interfere with occlusion of K+ in the E2[2K] conformation. Reduced phosphorylation levels or affinities for Na+ in presence of oligomycin indicate that Asp804 and Asp808 also contribute to coordination of Na+ in the E1P[3Na] form. Demonstration of alternate interactions of Na+ or K+ with Asp804 and Asp808 support the notion of cation binding in a ping‐pong sequence in catalytic models of Na,K‐pumping.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(96)01381-6</identifier><identifier>PMID: 9001399</identifier><language>eng</language><publisher>England</publisher><subject>Adenosine Triphosphate - metabolism ; Aspartic Acid ; Mutagenesis ; Mutagenesis, Site-Directed ; Na,K-ATPase ; Ouabain ; Ouabain - metabolism ; Potassium ; Potassium - metabolism ; Sodium ; Sodium - metabolism ; Sodium-Potassium-Exchanging ATPase - genetics ; Sodium-Potassium-Exchanging ATPase - metabolism ; Yeast expression ; Yeasts</subject><ispartof>FEBS letters, 1997-01, Vol.400 (2), p.206-210</ispartof><rights>FEBS Letters 400 (1997) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3126-73d0df9d7057992bb34ca1d3a338cd64c559ff2d570c6d6e37ccdaff88c7ba1e3</citedby></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%2896%2901381-6$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1016%2FS0014-5793%2896%2901381-6$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,1433,27924,27925,45574,45575,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9001399$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pedersen, Per Amstrup</creatorcontrib><creatorcontrib>Rasmussen, Jakob H</creatorcontrib><creatorcontrib>Nielsen, Jesper M</creatorcontrib><creatorcontrib>Jorgensen, Peter L</creatorcontrib><title>Identification of Asp804 and Asp808 as Na+ and K+ coordinating residues in α‐subunit of renal Na,K‐ATPase</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Mutations to Asp804 and Asp808 in the α‐subunit almost abolish Na,K‐ATPase activity, but high‐affinity binding of [3H]ATP or [3H]ouabain at equilibrium and E1–E2 transitions are preserved. Titration of K+‐ion displacement of [3H]ATP or [3H]ouabain shows that the mutations interfere with occlusion of K+ in the E2[2K] conformation. Reduced phosphorylation levels or affinities for Na+ in presence of oligomycin indicate that Asp804 and Asp808 also contribute to coordination of Na+ in the E1P[3Na] form. Demonstration of alternate interactions of Na+ or K+ with Asp804 and Asp808 support the notion of cation binding in a ping‐pong sequence in catalytic models of Na,K‐pumping.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>Aspartic Acid</subject><subject>Mutagenesis</subject><subject>Mutagenesis, Site-Directed</subject><subject>Na,K-ATPase</subject><subject>Ouabain</subject><subject>Ouabain - metabolism</subject><subject>Potassium</subject><subject>Potassium - metabolism</subject><subject>Sodium</subject><subject>Sodium - metabolism</subject><subject>Sodium-Potassium-Exchanging ATPase - genetics</subject><subject>Sodium-Potassium-Exchanging ATPase - metabolism</subject><subject>Yeast expression</subject><subject>Yeasts</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kF9OAjEQxhujQUSPQNJHDa62291u-4gEhEDURHxuuv1jaqBLtmwMbx7Bq3gRD-FJ3F0ITzPz_WYmMx8AfYzuMML0_hUhnERpxsk1pzcIE4YjegK6mGUkIgllp6B7bDkHFyF8oLpmmHdAh9cZ4bwL_Ewbv3XWKbl1hYeFhcOwYSiB0ut9yqAM8EkOWmU-gKooSu183e_fYWmC05UJ0Hn4-_P39R2qvPJu2ywqjZerevJ2XuvD5YsM5hKcWbkK5uoQe-BtMl6OptHi-XE2Gi4iRXBMo4xopC3XGaqP53Gek0RJrIkkhClNE5Wm3NpYpxlSVFNDMqW0tJYxleUSG9ID_f3eTZWvjRab0q1luROHv2s-3fNPtzK7I8ZINN6K1lvRGCc4Fa23gorJ-CFuSQM4bWVK_gHUGXCK</recordid><startdate>19970103</startdate><enddate>19970103</enddate><creator>Pedersen, Per Amstrup</creator><creator>Rasmussen, Jakob H</creator><creator>Nielsen, Jesper M</creator><creator>Jorgensen, Peter L</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope></search><sort><creationdate>19970103</creationdate><title>Identification of Asp804 and Asp808 as Na+ and K+ coordinating residues in α‐subunit of renal Na,K‐ATPase</title><author>Pedersen, Per Amstrup ; Rasmussen, Jakob H ; Nielsen, Jesper M ; Jorgensen, Peter L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3126-73d0df9d7057992bb34ca1d3a338cd64c559ff2d570c6d6e37ccdaff88c7ba1e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Adenosine Triphosphate - metabolism</topic><topic>Aspartic Acid</topic><topic>Mutagenesis</topic><topic>Mutagenesis, Site-Directed</topic><topic>Na,K-ATPase</topic><topic>Ouabain</topic><topic>Ouabain - metabolism</topic><topic>Potassium</topic><topic>Potassium - metabolism</topic><topic>Sodium</topic><topic>Sodium - metabolism</topic><topic>Sodium-Potassium-Exchanging ATPase - genetics</topic><topic>Sodium-Potassium-Exchanging ATPase - metabolism</topic><topic>Yeast expression</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pedersen, Per Amstrup</creatorcontrib><creatorcontrib>Rasmussen, Jakob H</creatorcontrib><creatorcontrib>Nielsen, Jesper M</creatorcontrib><creatorcontrib>Jorgensen, Peter L</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pedersen, Per Amstrup</au><au>Rasmussen, Jakob H</au><au>Nielsen, Jesper M</au><au>Jorgensen, Peter L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of Asp804 and Asp808 as Na+ and K+ coordinating residues in α‐subunit of renal Na,K‐ATPase</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1997-01-03</date><risdate>1997</risdate><volume>400</volume><issue>2</issue><spage>206</spage><epage>210</epage><pages>206-210</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Mutations to Asp804 and Asp808 in the α‐subunit almost abolish Na,K‐ATPase activity, but high‐affinity binding of [3H]ATP or [3H]ouabain at equilibrium and E1–E2 transitions are preserved. Titration of K+‐ion displacement of [3H]ATP or [3H]ouabain shows that the mutations interfere with occlusion of K+ in the E2[2K] conformation. Reduced phosphorylation levels or affinities for Na+ in presence of oligomycin indicate that Asp804 and Asp808 also contribute to coordination of Na+ in the E1P[3Na] form. Demonstration of alternate interactions of Na+ or K+ with Asp804 and Asp808 support the notion of cation binding in a ping‐pong sequence in catalytic models of Na,K‐pumping.</abstract><cop>England</cop><pmid>9001399</pmid><doi>10.1016/S0014-5793(96)01381-6</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 1997-01, Vol.400 (2), p.206-210 |
| issn | 0014-5793 1873-3468 |
| language | eng |
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| source | MEDLINE; Wiley Journals; Elsevier ScienceDirect Journals Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Wiley Free Content; Alma/SFX Local Collection |
| subjects | Adenosine Triphosphate - metabolism Aspartic Acid Mutagenesis Mutagenesis, Site-Directed Na,K-ATPase Ouabain Ouabain - metabolism Potassium Potassium - metabolism Sodium Sodium - metabolism Sodium-Potassium-Exchanging ATPase - genetics Sodium-Potassium-Exchanging ATPase - metabolism Yeast expression Yeasts |
| title | Identification of Asp804 and Asp808 as Na+ and K+ coordinating residues in α‐subunit of renal Na,K‐ATPase |
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