Interactions between Ca2+-ATPase and the pentameric form of phospholamban in two-dimensional co-crystals.

ABSTRACT: Phospholamban (PLB) physically interacts with Ca(2+)-ATPase and regulates contractility of the heart. We have studied this interaction using electron microscopy of large two-dimensional co-crystals of Ca(2+)-ATPase and the I40A mutant of PLB. Crystallization conditions were derived from those previously used for thin, helical crystals, but the addition of a 10-fold higher concentration of magnesium had a dramatic effect on the crystal morphology and packing. Two types of crystals were observed, and were characterized both by standard crystallographic methods and by electron tomography. The two crystal types had the same underlying lattice, which comprised antiparallel dimer ribbons of Ca(2+)-ATPase molecules previously seen in thin, helical crystals, but packed into a novel lattice with p2

SUBMITTER: Stokes DL 

PROVIDER: S-EPMC1459492 | biostudies-literature | 2006 Jun

REPOSITORIES: biostudies-literature