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

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  • Kim Langmach Hein, University of Oslo, Norway
  • Poul Nissen
  • Jens Preben Morth, Denmark
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.
Original languageEnglish
JournalActa Crystallographica. Section F: Structural Biology and Crystallization Communications Online
IssuePart 4
Pages (from-to)424-427
Number of pages4
Publication statusPublished - Apr 2012

    Research areas

  • Adenosine Triphosphatases, Amino Acid Sequence, Crystallization, Crystallography, X-Ray, Listeria monocytogenes, Models, Molecular, Protein Structure, Quaternary, Sequence Alignment

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