Encyclopedia of Metalloproteins

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

Calcium ATPase and Beryllium Fluoride

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



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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Copyright information

© Springer Science+Business Media New York 2013

Authors and Affiliations

  1. 1.Department of BiochemistryAsahikawa Medical UniversityAsahikawa, HokkaidoJapan