Open AccessPurification, crystallization and preliminary crystallographic studies of a PacL homologue from Listeria monocytogenes
Author(s) -
Hein Kim Langmach,
Nissen Poul,
Morth Jens Preben
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112004046
Subject(s) - crystallization , listeria monocytogenes , endoplasmic reticulum , serca , atpase , crystallography , chemistry , crystal (programming language) , bilayer , escherichia coli , molecular replacement , membrane , crystal structure , biochemistry , biology , enzyme , bacteria , gene , genetics , organic chemistry , computer science , programming language
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 P 2 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.