Unknown

Dataset Information

0

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


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.

SUBMITTER: Hein KL 

PROVIDER: S-EPMC3325811 | biostudies-literature | 2012 Apr

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Hein Kim Langmach KL   Nissen Poul P   Morth Jens Preben JP  

Acta crystallographica. Section F, Structural biology and crystallization communications 20120327 Pt 4


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 intermedia  ...[more]

Similar Datasets

| S-EPMC3976081 | biostudies-literature
| S-EPMC4188092 | biostudies-literature
| S-EPMC2705503 | biostudies-literature