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Structure and mecha...
Structure and mechanism of Zn2+-transporting P-type ATPases
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Wang, Kaituo (author)
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Sitsel, Oleg (author)
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Meloni, Gabriele (author)
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Autzen, Henriette Elisabeth (author)
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- Andersson, Magnus (author)
- KTH,Beräkningsbiofysik,Science for Life Laboratory, SciLifeLab,KTH, Beräkningsbiofysik
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Klymchuk, Tetyana (author)
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Nielsen, Anna Marie (author)
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Rees, Douglas C. (author)
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Nissen, Poul (author)
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- Gourdon, Pontus (author)
- Lund University,Lunds universitet,Medicinsk strukturbiologi,Forskargrupper vid Lunds universitet,Medical Structural Biology,Lund University Research Groups
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(creator_code:org_t)
- 2014-08-17
- 2014
- English.
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In: Nature. - : Springer Science and Business Media LLC. - 0028-0836 .- 1476-4687. ; 514:7523, s. 518-
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Abstract
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- Zinc is an essential micronutrient for all living organisms. It is required for signalling and proper functioning of a range of proteins involved in, for example, DNA binding and enzymatic catalysis(1). In prokaryotes and photosynthetic eukaryotes, Zn2+-transporting P-type ATPases of class IB (ZntA) are crucial for cellular redistribution and detoxification of Zn2+ and related elements(2,3). Here we present crystal structures representing the phosphoenzyme ground state (E2P) and a dephosphorylation intermediate (E2.P-i) of ZntA from Shigella sonnei, determined at 3.2 angstrom and 2.7 angstrom resolution, respectively. The structures reveal a similar fold to Cu+-ATPases, with an amphipathic helix at the membrane interface. A conserved electronegative funnel connects this region to the intramembranous high-affinity ion-binding site and may promote specific uptake of cellular Zn2+ ions by the transporter. The E2P structure displays a wide extracellular release pathway reaching the invariant residues at the high-affinity site, including C392, C394 and D714. The pathway closes in the E2.P-i state, in which D714 interacts with the conserved residue K693, which possibly stimulates Zn2+ release as a built-in counter ion, as has been proposed for H+-ATPases. Indeed, transport studies in liposomes provide experimental support for ZntA activity without counter transport. These findings suggest a mechanistic link between P-IB-type Zn2+-ATPases and P-III-type H+-ATPases and at the same time show structural features of the extracellular release pathway that resemble P-II-type ATPases such as the sarcoplasmic/endoplasmic reticulum Ca2+-ATPase(4,5) (SERCA) and Na+, K+-ATPase(6). These findings considerably increase our understanding of zinc transport in cells and represent new possibilities for biotechnology and biomedicine.
Subject headings
- NATURVETENSKAP -- Biologi -- Biofysik (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biophysics (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Cell- och molekylärbiologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Cell and Molecular Biology (hsv//eng)
Publication and Content Type
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Nature
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- By the author/editor
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Wang, Kaituo
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Sitsel, Oleg
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Meloni, Gabriele
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Autzen, Henriett ...
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Andersson, Magnu ...
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Klymchuk, Tetyan ...
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show more...
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Nielsen, Anna Ma ...
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Rees, Douglas C.
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Nissen, Poul
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Gourdon, Pontus
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show less...
- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Biophysics
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- MEDICAL AND HEALTH SCIENCES
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MEDICAL AND HEAL ...
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and Basic Medicine
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and Cell and Molecul ...
- Articles in the publication
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Nature
- By the university
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Royal Institute of Technology
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Lund University
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Umeå University