AI Article Synopsis
- Ca(2+)-ATPases are important membrane pumps that move calcium ions (Ca(2+)) across cell membranes, and the study focuses on LMCA1 from Listeria monocytogenes. * The LMCA1 was crystallized in a specific state (Ca(2+)-free) using aluminum fluoride (AlF(4)(-)), showcasing an intermediate state in its function. * The crystallization revealed a well-organized structure, with clear electron-density features, and the data provided insights into the protein's conformation and molecular arrangement.
Article 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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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3107152 | PMC |
| http://dx.doi.org/10.1107/S174430911101548X | DOI Listing |
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