Structure and Function of Cu(I)- and Zn(II)-ATPases

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Standard

Structure and Function of Cu(I)- and Zn(II)-ATPases. / Sitsel, Oleg; Grønberg, Christina; Autzen, Henriette Elisabeth; Wang, Kaituo; Meloni, Gabriele; Nissen, Poul; Gourdon, Pontus.

I: Biochemistry, Bind 54, Nr. 37, 22.09.2015, s. 5673-5683.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Sitsel, O, Grønberg, C, Autzen, HE, Wang, K, Meloni, G, Nissen, P & Gourdon, P 2015, 'Structure and Function of Cu(I)- and Zn(II)-ATPases', Biochemistry, bind 54, nr. 37, s. 5673-5683. https://doi.org/10.1021/acs.biochem.5b00512

APA

Sitsel, O., Grønberg, C., Autzen, H. E., Wang, K., Meloni, G., Nissen, P., & Gourdon, P. (2015). Structure and Function of Cu(I)- and Zn(II)-ATPases. Biochemistry, 54(37), 5673-5683. https://doi.org/10.1021/acs.biochem.5b00512

Vancouver

Sitsel O, Grønberg C, Autzen HE, Wang K, Meloni G, Nissen P o.a. Structure and Function of Cu(I)- and Zn(II)-ATPases. Biochemistry. 2015 sep. 22;54(37):5673-5683. https://doi.org/10.1021/acs.biochem.5b00512

Author

Sitsel, Oleg ; Grønberg, Christina ; Autzen, Henriette Elisabeth ; Wang, Kaituo ; Meloni, Gabriele ; Nissen, Poul ; Gourdon, Pontus. / Structure and Function of Cu(I)- and Zn(II)-ATPases. I: Biochemistry. 2015 ; Bind 54, Nr. 37. s. 5673-5683.

Bibtex

@article{046ce6e27f8b4d9288d6c1032674de09,
title = "Structure and Function of Cu(I)- and Zn(II)-ATPases",
abstract = "Copper and zinc are micronutrients essential for the function of many enzymes while also being toxic at elevated concentrations. Cu(I)- and Zn(II)-transporting P-type ATPases of subclass 1B are of key importance for the homeostasis of these transition metals, allowing ion transport across cellular membranes at the expense of ATP. Recent biochemical studies and crystal structures have significantly improved our understanding of the transport mechanisms of these proteins, but many details about their structure and function remain elusive. Here we compare the Cu(I)- and Zn(II)-ATPases, scrutinizing the molecular differences that allow transport of these two distinct metal types, and discuss possible future directions of research in the field.",
author = "Oleg Sitsel and Christina Gr{\o}nberg and Autzen, {Henriette Elisabeth} and Kaituo Wang and Gabriele Meloni and Poul Nissen and Pontus Gourdon",
year = "2015",
month = sep,
day = "22",
doi = "10.1021/acs.biochem.5b00512",
language = "English",
volume = "54",
pages = "5673--5683",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "37",

}

RIS

TY - JOUR

T1 - Structure and Function of Cu(I)- and Zn(II)-ATPases

AU - Sitsel, Oleg

AU - Grønberg, Christina

AU - Autzen, Henriette Elisabeth

AU - Wang, Kaituo

AU - Meloni, Gabriele

AU - Nissen, Poul

AU - Gourdon, Pontus

PY - 2015/9/22

Y1 - 2015/9/22

N2 - Copper and zinc are micronutrients essential for the function of many enzymes while also being toxic at elevated concentrations. Cu(I)- and Zn(II)-transporting P-type ATPases of subclass 1B are of key importance for the homeostasis of these transition metals, allowing ion transport across cellular membranes at the expense of ATP. Recent biochemical studies and crystal structures have significantly improved our understanding of the transport mechanisms of these proteins, but many details about their structure and function remain elusive. Here we compare the Cu(I)- and Zn(II)-ATPases, scrutinizing the molecular differences that allow transport of these two distinct metal types, and discuss possible future directions of research in the field.

AB - Copper and zinc are micronutrients essential for the function of many enzymes while also being toxic at elevated concentrations. Cu(I)- and Zn(II)-transporting P-type ATPases of subclass 1B are of key importance for the homeostasis of these transition metals, allowing ion transport across cellular membranes at the expense of ATP. Recent biochemical studies and crystal structures have significantly improved our understanding of the transport mechanisms of these proteins, but many details about their structure and function remain elusive. Here we compare the Cu(I)- and Zn(II)-ATPases, scrutinizing the molecular differences that allow transport of these two distinct metal types, and discuss possible future directions of research in the field.

U2 - 10.1021/acs.biochem.5b00512

DO - 10.1021/acs.biochem.5b00512

M3 - Journal article

C2 - 26132333

VL - 54

SP - 5673

EP - 5683

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 37

ER -

ID: 144248508