Purification, crystallization and preliminary crystallographic studies of a PacL homologue from Listeria monocytogenes.
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.
Centre for Molecular Medicine Norway, University of Oslo, PO Box 1137 Blindern, 0318 Oslo, Norway. firstname.lastname@example.org
SourceActa crystallographica. Section F, Structural biology and crystallization communications 68:Pt 4 2012 Apr 1 pg 424-7
Amino Acid Sequence
Protein Structure, Quaternary
Pub Type(s)Journal Article
Research Support, Non-U.S. Gov't