title: Crystallization and preliminary structural analysis of the Listeria monocytogenes Ca(2+)-ATPase LMCA1.
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.
authors.affiliation: Centre for Membrane Pumps in Cells and Disease-PUMPKIN, University of Aarhus, Gustav Wieds Vej 10C, Aarhus C, Denmark.
authors.forename: Jacob Lauwring
authors.initials: JL
authors.lastname: Andersen
authors.forename: Pontus
authors.initials: P
authors.lastname: Gourdon
authors.forename: Jesper Vuust
authors.initials: JV
authors.lastname: Møller
authors.forename: Jens Preben
authors.initials: JP
authors.lastname: Morth
authors.forename: Poul
authors.initials: P
authors.lastname: Nissen
mesh_terms: D000252:Calcium-Transporting ATPases / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D008089:Listeria monocytogenes / Q000201:enzymology*; D008958:Models, Molecular; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary
chemical_list: D000252:Calcium-Transporting ATPases