Electron microscopic analysis of two-dimensional crystals of the Ca2+-transport ATPase - a freeze-fracture study

H. Ping Ting-Beall, Florence M. Burgess, L. Dux, Anthony Martonosi

Research output: Contribution to journalArticle

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Abstract

Two distinct forms of Ca2+-ATPase crystals have been analysed in sarcoplasmic reticulum (SR) membranes. The E1-type crystals, induced by Ca2+ or lanthanide ions, consist of single chains of ATPase monomers, and the E2-type crystals, induced by vanadate ions, consist of dimer chains. Using improved freeze-fracture techniques we have obtained high-resolution images of complementary surface replicas of SR membranes containing these crystal forms. In E1 crystals, the concave fracture (P) faces display obliquely oriented rows of intramembrane particles (IMPs) spaced at ∼- 6-7 nm along both crystal axes, while the convex fracture (E) faces show corresponding rows of pits. In E2 crystals, regular arrays of oblique parallel ridges with spacing of ∼- 10.5-11 nm appear on the P-faces and complementary grooves or furrows on the E-faces. In many instances the ridges break up into elongated particles repeating every 5.5 nm. When the direction of the shadow is almost parallel to the axis of the ridges, these 9.5 nm particles can be resolved into two domains, which represent intramembranous contacts between the two monomers of the two adjacent dimer chains. Complementary grooves on the E-faces can also be resolved into rows of pits complementary to the particles of the ridges on the P-faces. In the control SR membranes, randomly dispersed IMPs and corresponding pits are observed on the P- and E-faces, respectively. The data suggest that transport of Ca2+ involves significant structural changes of the enzyme molecule, reflected in the ATPase-ATPase interactions both on the cytoplasmic surface and in the lipid bilayer.

Original languageEnglish
Pages (from-to)252-259
Number of pages8
JournalJournal of Muscle Research and Cell Motility
Volume8
Issue number3
DOIs
Publication statusPublished - Jun 1987

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Calcium-Transporting ATPases
Sarcoplasmic Reticulum
Adenosine Triphosphatases
Electrons
Crystals
Membranes
Ions
Lanthanoid Series Elements
Vanadates
Lipid Bilayers
Dimers
Monomers
Enzymes
Lipid bilayers
Image resolution
Display devices
Molecules

ASJC Scopus subject areas

  • Physiology
  • Endocrinology
  • Clinical Biochemistry
  • Cell Biology

Cite this

Electron microscopic analysis of two-dimensional crystals of the Ca2+-transport ATPase - a freeze-fracture study. / Ting-Beall, H. Ping; Burgess, Florence M.; Dux, L.; Martonosi, Anthony.

In: Journal of Muscle Research and Cell Motility, Vol. 8, No. 3, 06.1987, p. 252-259.

Research output: Contribution to journalArticle

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