ArticleActa crystallographica. Section F, Structural biology and crystallization communications2011
Crystallization and preliminary structural analysis of the Listeria monocytogenes Ca(2+)-ATPase LMCA1.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed.
- Unveiling the Secrets of Calcium-Dependent Proteins in Plant Growth-Promoting Rhizobacteria: An Abundance of Discoveries Awaits.Plants (Basel, Switzerland) · 2023Review
- Characterization of CaBiochimica et biophysica acta. Biomembranes · 2023Article
- Chimeric Claudins: A New Tool to Study Tight Junction Structure and Function.International journal of molecular sciences · 2021Article
- Be Cautious with Crystal Structures of Membrane Proteins or Complexes Prepared in Detergents.Crystals · 2020Article
- Article
- Engineering a Prototypic P-type ATPase Listeria monocytogenes Ca(2+)-ATPase 1 for Single-Molecule FRET Studies.Bioconjugate chemistry · 2016Article
- Purification, crystallization and preliminary crystallographic studies of a PacL homologue from Listeria monocytogenes.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
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5 authors.
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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.
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