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Structure and mechanism of Zn2+-transporting P-type ATPases
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2014 (Engelska)Ingår i: Nature, ISSN 0028-0836, E-ISSN 1476-4687, Vol. 514, nr 7523, s. 518-+Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

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.

Ort, förlag, år, upplaga, sidor
2014. Vol. 514, nr 7523, s. 518-+
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Biofysik
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URN: urn:nbn:se:kth:diva-156441DOI: 10.1038/nature13618ISI: 000343775900046OAI: oai:DiVA.org:kth-156441DiVA, id: diva2:767986
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QC 20141202

Tillgänglig från: 2014-12-02 Skapad: 2014-11-28 Senast uppdaterad: 2017-12-05Bibliografiskt granskad

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Andersson, Magnus

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BeräkningsbiofysikScience for Life Laboratory, SciLifeLab
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