Crystallization and preliminary structural analysis of the Listeria monocytogenes Ca(2+)-ATPase LMCA1

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jun 1;67(Pt 6):718-22. doi: 10.1107/S174430911101548X. Epub 2011 May 26.

Abstract

Ca(2+)-ATPases are ATP-driven membrane pumps that are responsible for the transport of Ca(2+) ions across the membrane. The Listeria monocytogenes Ca(2+)-ATPase LMCA1 has been crystallized in the Ca(2+)-free state stabilized by AlF(4)(-), representing an occluded E2-P(i)-like state. The crystals belonged to space group P2(1)2(1)2 and a complete data set extending to 4.3 Å resolution was collected. A molecular-replacement solution was obtained, revealing type I packing of the molecules in the crystal. Unbiased electron-density features were observed for AlF(4)(-) and for shifts of the helices, which were indicative of a reliable structure determination.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Calcium-Transporting ATPases / chemistry*
  • Calcium-Transporting ATPases / isolation & purification
  • Crystallization
  • Crystallography, X-Ray
  • Listeria monocytogenes / enzymology*
  • Models, Molecular
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary

Substances

  • Calcium-Transporting ATPases