Three-dimensional cryo-electron microscopy of the calcium ion pump in the sarcoplasmic reticulum membrane
Article Abstract:
The three-dimensional structure of the ATP-driven calcium pump (Ca-ATPase) of the sarcoplasmic reticulum was determined by cryo-electron microscopy and helical image analysis. The results showed that Ca-ATPase consists of cytoplasmic, transmembrane and luminal parts, with a height of 120 angstroms. The transmembrane domain showed three distinct segments, one of which is highly inclined. These and other findings were related to the previously determined secondary structure of the protein.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
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Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues
Article Abstract:
A study is conducted to report, at 2.3 angstrom, the structure of the calcium-ATPase of skeletal muscle sarcoplasmic reticulum, a representative P-type ATPase that is crystallized in the absence of Ca(super 2+) but in the presence of magnesium fluoride, a stable phosphate analogue. This and other crystal structures determined previously provide atomic models for all four principal states in the reaction cycle.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2004
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Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution
Article Abstract:
It has been possible to describe the atomic model of Ca2+-ATPase with bound Ca2+ on the basis of X-ray diffraction data at 2.6 angstrom resolution. The cytoplasmic region was found to consist of three well separated domains.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2000
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