Purification, crystallization and preliminary crystallographic studies of a PacL homologue from Listeria monocytogenes

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  • Kim Langmach Hein, University of Oslo, Norge
  • Poul Nissen
  • Jens Preben Morth, Danmark
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.
TidsskriftActa Crystallographica. Section F: Structural Biology and Crystallization Communications Online
NummerPart 4
Sider (fra-til)424-427
Antal sider4
StatusUdgivet - apr. 2012

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