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Crystallization and preliminary structural analysis of the Listeria monocytogenes Ca(2+)-ATPase LMCA1.

ABSTRACT: Ca(2+)-ATPases are ATP-driven membrane pumps that are responsible for the transport of Ca(2+) ions across the membrane. The Listeria monocytogenes Ca(2+)-ATPase LMCA1 has been crystallized in the Ca(2+)-free state stabilized by AlF(4)(-), representing an occluded E2-P(i)-like state. The crystals belonged to space group P2(1)2(1)2 and a complete data set extending to 4.3?Å resolution was collected. A molecular-replacement solution was obtained, revealing type I packing of the molecules in the crystal. Unbiased electron-density features were observed for AlF(4)(-) and for shifts of the helices, which were indicative of a reliable structure determination.

SUBMITTER: Andersen JL

PROVIDER: S-EPMC3107152 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature

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Crystallization and preliminary structural analysis of the Listeria monocytogenes Ca(2+)-ATPase LMCA1.

Andersen Jacob Lauwring JL Gourdon Pontus P Møller Jesper Vuust JV Morth Jens Preben JP Nissen Poul P

Acta crystallographica. Section F, Structural biology and crystallization communications 20110526 Pt 6

Ca(2+)-ATPases are ATP-driven membrane pumps that are responsible for the transport of Ca(2+) ions across the membrane. The Listeria monocytogenes Ca(2+)-ATPase LMCA1 has been crystallized in the Ca(2+)-free state stabilized by AlF(4)(-), representing an occluded E2-P(i)-like state. The crystals belonged to space group P2(1)2(1)2 and a complete data set extending to 4.3 Å resolution was collected. A molecular-replacement solution was obtained, revealing type I packing of the molecules in the cry ...[more]

PMID: 21636921

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