Encyclopedia of Metalloproteins

2013 Edition
| Editors: Robert H. Kretsinger, Vladimir N. Uversky, Eugene A. Permyakov

Calcium ATPase and Beryllium Fluoride

Reference work entry
DOI: https://doi.org/10.1007/978-1-4614-1533-6_173

Synonyms

Definition

Sarco(endo)plasmic reticulum Ca2+-ATPase, calcium pump, catalyzes Ca2+ transport coupled with ATP hydrolysis into the lumen against ∼10,000 time concentration gradient. The ATPase is activated by high-affinity binding of two cytoplasmic Ca2+ ions at the transport sites in the transmembrane region and forms an autophosphorylated intermediate by transferring ATP γ-phosphate to a catalytic aspartate (Asp351) in the cytoplasmic region. The subsequent large conformational change disrupts the Ca2+ binding sites and releases Ca2+ into the lumen and produces the catalytic site for hydrolysis of the Asp351-phosphate bond. Beryllium in beryllium fluoride (BeF3) compound is directly ligated with the catalytic aspartyl oxygen, producing a very stable analog of the covalently bound phosphate at Asp351 with an equivalent tetrahedral structure and bond lengths. The biochemical studies of the Ca2+-ATPase/BeF3 complexes with and without bound Ca2+at the transport...

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References

  1. Daiho T, Yamasaki K, Danko S, Suzuki H (2007) Critical role of Glu40-Ser48 loop linking actuator domain and 1st transmembrane helix of Ca2+-ATPase in Ca2+ deocclusion and release from ADP-insensitive phosphoenzyme. J Biol Chem 282:34429–34447CrossRefPubMedGoogle Scholar
  2. Daiho T, Danko S, Yamasaki K, Suzuki H (2010) Stable structural analog of Ca2+-ATPase ADP-insensitive phosphoenzyme with occluded Ca2+ formed by elongation of A-domain/M1’-linker and beryllium fluoride binding. J Biol Chem 285:24538–24547CrossRefPubMedGoogle Scholar
  3. Danko S, Yamasaki K, Daiho T, Suzuki H (2004) Distinct natures of beryllium fluoride-bound, aluminum fluoride-bound, and magnesium fluoride-bound stable analogues of an ADP-insensitive phosphoenzyme intermediate of sarcoplasmic reticulum Ca2+-ATPase CHANGES IN CATALYTIC AND TRANSPORT SITES DURING PHOSPHOENZYME HYDROLYSIS. J Biol Chem 279:14991–14998CrossRefPubMedGoogle Scholar
  4. Danko S, Daiho T, Yamasaki K, Liu X, Suzuki H (2009) Formation of stable structural analog of ADP-sensitive phosphoenzyme of Ca2+-ATPase with occluded Ca2+ by beryllium fluoride STRUCTURAL CHANGES DURING PHOSPHORYLATION AND ISOMERIZATION. J Biol Chem 284:22722–22735CrossRefPubMedGoogle Scholar
  5. Møller JV, Olesen C, Winther AM, Nissen P (2010) The sarcoplasmic Ca2+-ATPase: design of a perfect chemi-osmotic pump. Q Rev Biophys 43:501–56CrossRefPubMedGoogle Scholar
  6. Olesen C, Picard M, Winther AM, Gyrup C, Morth JP, Oxvig C, Møller JV, Nissen P (2007) The structural basis of calcium transport by the calcium pump. Nature 450:1036–42CrossRefPubMedGoogle Scholar
  7. Toyoshima C (2008) Structural aspects of ion pumping by Ca2+-ATPase of sarcoplasmic reticulum. Arch Biochem Biophys 476:3–11CrossRefPubMedGoogle Scholar
  8. Toyoshima C (2009) How Ca2+-ATPase pumps ions across the sarcoplasmic reticulum membrane. Biochim Biophys Acta 1793:941–946CrossRefPubMedGoogle Scholar
  9. Toyoshima C, Norimatsu Y, Iwasawa S, Tsuda T, Ogawa H (2007) How processing of aspartylphosphate is coupled to lumenal gating of the ion pathway in the calcium pump. Proc Natl Acad Sci USA 104:19831–19836CrossRefPubMedGoogle Scholar
  10. Yamasaki K, Wang G, Daiho T, Danko S, Suzuki H (2008) Roles of Tyr122-hydrophobic cluster and K+ binding in Ca2+-releasing process of ADP-insensitive phosphoenzyme of sarcoplasmic reticulum Ca2+-ATPase. J Biol Chem 283:29144–29155CrossRefPubMedGoogle Scholar

Copyright information

© Springer Science+Business Media New York 2013

Authors and Affiliations

  1. 1.Department of BiochemistryAsahikawa Medical UniversityAsahikawa, HokkaidoJapan