On allosteric modulation of P-type Cu(+)-ATPases

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On allosteric modulation of P-type Cu(+)-ATPases. / Mattle, Daniel; Sitsel, Oleg; Autzen, Henriette Elisabeth; Meloni, Gabriele; Gourdon, Pontus; Nissen, Poul.

I: Journal of Molecular Biology, Vol. 425, Nr. 13, 10.07.2013, s. 2299-308.

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

Harvard

Mattle, D, Sitsel, O, Autzen, HE, Meloni, G, Gourdon, P & Nissen, P 2013, 'On allosteric modulation of P-type Cu(+)-ATPases', Journal of Molecular Biology, vol. 425, nr. 13, s. 2299-308. https://doi.org/10.1016/j.jmb.2013.03.008

APA

Mattle, D., Sitsel, O., Autzen, H. E., Meloni, G., Gourdon, P., & Nissen, P. (2013). On allosteric modulation of P-type Cu(+)-ATPases. Journal of Molecular Biology, 425(13), 2299-308. https://doi.org/10.1016/j.jmb.2013.03.008

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MLA

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Author

Mattle, Daniel ; Sitsel, Oleg ; Autzen, Henriette Elisabeth ; Meloni, Gabriele ; Gourdon, Pontus ; Nissen, Poul. / On allosteric modulation of P-type Cu(+)-ATPases. I: Journal of Molecular Biology. 2013 ; Vol. 425, Nr. 13. s. 2299-308.

RIS

TY - JOUR

T1 - On allosteric modulation of P-type Cu(+)-ATPases

AU - Mattle, Daniel

AU - Sitsel, Oleg

AU - Autzen, Henriette Elisabeth

AU - Meloni, Gabriele

AU - Gourdon, Pontus

AU - Nissen, Poul

N1 - Copyright © 2013 Elsevier Ltd. All rights reserved.

PY - 2013/7/10

Y1 - 2013/7/10

N2 - P-type ATPases perform active transport of various compounds across biological membranes and are crucial for ion homeostasis and the asymmetric composition of lipid bilayers. Although their functional cycle share principles of phosphoenzyme intermediates, P-type ATPases also show subclass-specific sequence motifs and structural elements that are linked to transport specificity and mechanistic modulation. Here we provide an overview of the Cu(+)-transporting ATPases (of subclass PIB) and compare them to the well-studied sarco(endo)plasmic reticulum Ca(2+)-ATPase (of subclass PIIA). Cu(+) ions in the cell are delivered by soluble chaperones to Cu(+)-ATPases, which expose a putative "docking platform" at the intracellular interface. Cu(+)-ATPases also contain heavy-metal binding domains providing a basis for allosteric control of pump activity. Database analysis of Cu(+) ligating residues questions a two-site model of intramembranous Cu(+) binding, and we suggest an alternative role for the proposed second site in copper translocation and proton exchange. The class-specific features demonstrate that topological diversity in P-type ATPases may tune a general energy coupling scheme to the translocation of compounds with remarkably different properties.

AB - P-type ATPases perform active transport of various compounds across biological membranes and are crucial for ion homeostasis and the asymmetric composition of lipid bilayers. Although their functional cycle share principles of phosphoenzyme intermediates, P-type ATPases also show subclass-specific sequence motifs and structural elements that are linked to transport specificity and mechanistic modulation. Here we provide an overview of the Cu(+)-transporting ATPases (of subclass PIB) and compare them to the well-studied sarco(endo)plasmic reticulum Ca(2+)-ATPase (of subclass PIIA). Cu(+) ions in the cell are delivered by soluble chaperones to Cu(+)-ATPases, which expose a putative "docking platform" at the intracellular interface. Cu(+)-ATPases also contain heavy-metal binding domains providing a basis for allosteric control of pump activity. Database analysis of Cu(+) ligating residues questions a two-site model of intramembranous Cu(+) binding, and we suggest an alternative role for the proposed second site in copper translocation and proton exchange. The class-specific features demonstrate that topological diversity in P-type ATPases may tune a general energy coupling scheme to the translocation of compounds with remarkably different properties.

KW - Adenosine Triphosphatases

KW - Allosteric Regulation

KW - Binding Sites

KW - Cation Transport Proteins

KW - Crystallography, X-Ray

KW - Ion Transport

KW - Models, Biological

KW - Models, Molecular

KW - Molecular Dynamics Simulation

KW - Protein Conformation

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

KW - Review

U2 - 10.1016/j.jmb.2013.03.008

DO - 10.1016/j.jmb.2013.03.008

M3 - Article

VL - 425

SP - 2299

EP - 2308

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 1089-8638

IS - 13

ER -