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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
45
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pubmed:dateCreated |
2004-11-1
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pubmed:databankReference |
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pubmed:abstractText |
K+ plays an important role for the function of the sarco(endo)plasmic reticulum Ca2+ -ATPase (SERCA), but its binding site within the molecule has remained unidentified. We have located the binding site for a K+ ion in the P-domain by means of x-ray crystallography using crystals prepared in the presence of the K+ congener Rb+. Backbone carbonyls from the loop containing residues 711-715 together with the side chain of Glu732 define the K+/Rb+ site in the Ca2+ -ATPase conformation with bound Ca2+, ADP, and AlF4-. Functional analysis of Ca2+ -ATPase mutants with alterations to Glu732 shows that this site is indeed important for the stimulatory effect of K+ on the dephosphorylation rate. Comparison with the Ca2+ -ATPase in a dephosphorylated E2 conformation suggests that the K+ site is involved in the correct movement and positioning of the A-domain during translocation and dephosphorylation.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
279
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
46355-8
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:15383548-Adenosine Diphosphate,
pubmed-meshheading:15383548-Adenosine Triphosphatases,
pubmed-meshheading:15383548-Amino Acid Sequence,
pubmed-meshheading:15383548-Animals,
pubmed-meshheading:15383548-Binding Sites,
pubmed-meshheading:15383548-COS Cells,
pubmed-meshheading:15383548-Calcium-Transporting ATPases,
pubmed-meshheading:15383548-Crystallography, X-Ray,
pubmed-meshheading:15383548-Cytoplasm,
pubmed-meshheading:15383548-DNA, Complementary,
pubmed-meshheading:15383548-Electrons,
pubmed-meshheading:15383548-Glutamic Acid,
pubmed-meshheading:15383548-Models, Molecular,
pubmed-meshheading:15383548-Molecular Sequence Data,
pubmed-meshheading:15383548-Muscle, Skeletal,
pubmed-meshheading:15383548-Mutagenesis, Site-Directed,
pubmed-meshheading:15383548-Mutation,
pubmed-meshheading:15383548-Phosphorylation,
pubmed-meshheading:15383548-Potassium,
pubmed-meshheading:15383548-Protein Conformation,
pubmed-meshheading:15383548-Protein Structure, Tertiary,
pubmed-meshheading:15383548-Protein Transport,
pubmed-meshheading:15383548-Rabbits,
pubmed-meshheading:15383548-Sarcoplasmic Reticulum,
pubmed-meshheading:15383548-Sarcoplasmic Reticulum Calcium-Transporting ATPases,
pubmed-meshheading:15383548-Time Factors
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pubmed:year |
2004
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pubmed:articleTitle |
Localization of a K+ -binding site involved in dephosphorylation of the sarcoplasmic reticulum Ca2+ -ATPase.
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pubmed:affiliation |
Centre for Structural Biology, Department of Molecular Biology, University of Aarhus, Gustav Wieds Vej 10C, DK-8000 Aarhus C, Denmark.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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