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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
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
Wiley-Blackwell
external identifiers
  • scopus:79958123833
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
2017-08-27 06:40:03
@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},
  keyword      = {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    = {Wiley-Blackwell},
  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},
  volume       = {67},
  year         = {2011},
}