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

Andersen, Jacob Lauwring ; Gourdon, Pontus LU ; Møller, Jesper Vuust ; Morth, Jens Preben and Nissen, Poul (2011) In Acta crystallographica. Section F, Structural biology communications 67(Pt 6). p.22-718
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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author
; ; ; and
publishing date
type
Contribution to journal
publication status
published
keywords
Calcium-Transporting ATPases, Crystallization, Crystallography, X-Ray, Listeria monocytogenes, Models, Molecular, Protein Structure, Quaternary, Protein Structure, Tertiary, Journal Article, Research Support, Non-U.S. Gov't
in
Acta crystallographica. Section F, Structural biology communications
volume
67
issue
Pt 6
pages
22 - 718
publisher
John Wiley & Sons Inc.
external identifiers
  • scopus:79958123833
  • pmid:21636921
ISSN
2053-230X
DOI
10.1107/S174430911101548X
language
English
LU publication?
no
id
35e3627c-3f2f-4d66-91b2-fdc7b4cece94
date added to LUP
2017-04-29 15:31:38
date last changed
2025-01-07 12:11:27
@article{35e3627c-3f2f-4d66-91b2-fdc7b4cece94,
  abstract     = {{<p>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.</p>}},
  author       = {{Andersen, Jacob Lauwring and Gourdon, Pontus and Møller, Jesper Vuust and Morth, Jens Preben and Nissen, Poul}},
  issn         = {{2053-230X}},
  keywords     = {{Calcium-Transporting ATPases; Crystallization; Crystallography, X-Ray; Listeria monocytogenes; Models, Molecular; Protein Structure, Quaternary; Protein Structure, Tertiary; Journal Article; Research Support, Non-U.S. Gov't}},
  language     = {{eng}},
  month        = {{06}},
  number       = {{Pt 6}},
  pages        = {{22--718}},
  publisher    = {{John Wiley & Sons Inc.}},
  series       = {{Acta crystallographica. Section F, Structural biology communications}},
  title        = {{Crystallization and preliminary structural analysis of the Listeria monocytogenes Ca(2+)-ATPase LMCA1}},
  url          = {{http://dx.doi.org/10.1107/S174430911101548X}},
  doi          = {{10.1107/S174430911101548X}},
  volume       = {{67}},
  year         = {{2011}},
}