title: Purification, crystallization and preliminary crystallographic studies of a PacL homologue from Listeria monocytogenes.
abstract: Ca(2+)-ATPases are members of a large family of membrane proteins that maintain the selective movement of cations across biological membranes. A putative Listeria monocytogenes Ca(2+)-ATPase (Lmo0818) was crystallized in an unknown functional state. The crystal belonged to space group P2(1)2(1)2(1) and a complete data set was collected to 3.2 Å resolution. The molecular-replacement solution obtained revealed that Lmo0818 is likely to adopt an E2-like state mimicking the phosphorylated intermediate in the functional cycle of the sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA) and a stacked bilayer `type I' packing in the crystal.
authors.affiliation: Centre for Molecular Medicine Norway, University of Oslo, PO Box 1137 Blindern, 0318 Oslo, Norway. kimlan@ncmm.uio.no
authors.forename: Kim Langmach
authors.initials: KL
authors.lastname: Hein
authors.forename: Poul
authors.initials: P
authors.lastname: Nissen
authors.forename: Jens Preben
authors.initials: JP
authors.lastname: Morth
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000302:isolation & purification; D000595:Amino Acid Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D008089:Listeria monocytogenes / Q000201:enzymology*; D008958:Models, Molecular; D020836:Protein Structure, Quaternary; D016415:Sequence Alignment
chemical_list: D000251:Adenosine Triphosphatases