Structure and ion-release mechanism of PIB-4-type ATPases
Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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Structure and ion-release mechanism of PIB-4-type ATPases. / Grønberg, Christina; Hu, Qiaoxia; Mahato, Dhani Ram; Longhin, Elena; Salustros, Nina; Duelli, Annette; Lyu, Pin; Bågenholm, Viktoria; Eriksson, Jonas; Rao, Komal Umashankar; Henderson, Domhnall Iain; Meloni, Gabriele; Andersson, Magnus; Croll, Tristan; Godaly, Gabriela; Wang, Kaituo; Gourdon, Pontus.
I: eLife, Bind 10, e73124, 12.2021.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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T1 - Structure and ion-release mechanism of PIB-4-type ATPases
AU - Grønberg, Christina
AU - Hu, Qiaoxia
AU - Mahato, Dhani Ram
AU - Longhin, Elena
AU - Salustros, Nina
AU - Duelli, Annette
AU - Lyu, Pin
AU - Bågenholm, Viktoria
AU - Eriksson, Jonas
AU - Rao, Komal Umashankar
AU - Henderson, Domhnall Iain
AU - Meloni, Gabriele
AU - Andersson, Magnus
AU - Croll, Tristan
AU - Godaly, Gabriela
AU - Wang, Kaituo
AU - Gourdon, Pontus
N1 - Publisher Copyright: © 2021, eLife Sciences Publications Ltd. All rights reserved.
PY - 2021/12
Y1 - 2021/12
N2 - Transition metals, such as zinc, are essential micronutrients in all organisms, but also highly toxic in excessive amounts. Heavy-metal transporting P-type (PIB) ATPases are crucial for homeostasis, conferring cellular detoxification and redistribution through transport of these ions across cellular membranes. No structural information is available for the PIB-4-ATPases, the subclass with the broadest cargo scope, and hence even their topology remains elusive. Here we present structures and complementary functional analyses of an archetypal PIB-4-ATPase, sCoaT from Sulfitobacter sp. NAS14-1. The data disclose the architecture, devoid of classical so-called heavy metal binding domains, and provides fundamentally new insights into the mechanism and diversity of heavy metal transporters. We reveal several novel P-type ATPase features, including a dual role in heavy-metal release and as an internal counter ion of an invariant Page 2 histidine. We also establish that the turn-over of PIB-ATPases is potassium independent, contrasting to many other P-type ATPases. Combined with new inhibitory compounds, our results open up for efforts in e.g. drug discovery, since PIB-4-ATPases function as virulence factors in many pathogens.
AB - Transition metals, such as zinc, are essential micronutrients in all organisms, but also highly toxic in excessive amounts. Heavy-metal transporting P-type (PIB) ATPases are crucial for homeostasis, conferring cellular detoxification and redistribution through transport of these ions across cellular membranes. No structural information is available for the PIB-4-ATPases, the subclass with the broadest cargo scope, and hence even their topology remains elusive. Here we present structures and complementary functional analyses of an archetypal PIB-4-ATPase, sCoaT from Sulfitobacter sp. NAS14-1. The data disclose the architecture, devoid of classical so-called heavy metal binding domains, and provides fundamentally new insights into the mechanism and diversity of heavy metal transporters. We reveal several novel P-type ATPase features, including a dual role in heavy-metal release and as an internal counter ion of an invariant Page 2 histidine. We also establish that the turn-over of PIB-ATPases is potassium independent, contrasting to many other P-type ATPases. Combined with new inhibitory compounds, our results open up for efforts in e.g. drug discovery, since PIB-4-ATPases function as virulence factors in many pathogens.
UR - http://www.scopus.com/inward/record.url?scp=85122387723&partnerID=8YFLogxK
U2 - 10.7554/eLife.73124
DO - 10.7554/eLife.73124
M3 - Journal article
C2 - 34951590
AN - SCOPUS:85122387723
VL - 10
JO - eLife
JF - eLife
SN - 2050-084X
M1 - e73124
ER -
ID: 290181197