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.

Links

Publisher Full Text

Authors

Hein KL, Nissen P, Morth JP

Institution

Centre for Molecular Medicine Norway, University of Oslo, PO Box 1137 Blindern, 0318 Oslo, Norway. kimlan@ncmm.uio.no

Source

Acta crystallographica. Section F, Structural biology and crystallization communications 68:Pt 4 2012 Apr 1 pg 424-7

MeSH

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

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

22505411