Co-reconstitution and Co-crystallization of phospholamban and Ca2+-ATPase

Howard S. Young, Laxma G. Reddy, Larry R. Jones, David L. Stokes

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


Significant advances have recently been made in understanding the regulation of Ca2+-ATPase by phospholamban and in modeling their structures. However, these insights would be furthered by determining the 3-D structure of both proteins within the membrane, thus revealing the structural basis for their interaction. To this end, we have developed methods for reconstituting purified Ca2+-ATPase with recombinant phospholamban. After reconstitution at high lipid-to-protein ratios, we have verified their functional association by measuring calcium transport and ATPase activity. Furthermore, we have grown co-crystals after reconstitution at low lipid-to-protein ratios. The structure of Ca2+-ATPase has recently been solved by cryoelectron microscopy at 8-Å resolution, thus revealing transmembrane α-helices. Using a variety of constraints, we have associated these helices with the predicted transmembrane sequences to produce a detailed model for the packing of transmembrane helices. Structure determination of the co-crystals is currently underway, which we hope will eventually reveal the interaction of phospholamban with Ca2+-ATPase at a similar level of detail.

Original languageEnglish (US)
Pages (from-to)103-115
Number of pages13
JournalAnnals of the New York Academy of Sciences
StatePublished - 1998

ASJC Scopus subject areas

  • Neuroscience(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • History and Philosophy of Science

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