Crystal structure of a copper-transporting PIB-type ATPase

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Crystal structure of a copper-transporting PIB-type ATPase. / Gourdon, Pontus Emanuel; Liu, Xiang-Yu; Skjørringe, Tina; Morth, J Preben; Møller, Lisbeth Birk; Pedersen, Bjørn Panyella; Nissen, Poul.

In: Nature, Vol. 475, No. 7354, 07.07.2011, p. 59-64.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Gourdon, PE, Liu, X-Y, Skjørringe, T, Morth, JP, Møller, LB, Pedersen, BP & Nissen, P 2011, 'Crystal structure of a copper-transporting PIB-type ATPase', Nature, vol. 475, no. 7354, pp. 59-64. https://doi.org/10.1038/nature10191

APA

Gourdon, P. E., Liu, X-Y., Skjørringe, T., Morth, J. P., Møller, L. B., Pedersen, B. P., & Nissen, P. (2011). Crystal structure of a copper-transporting PIB-type ATPase. Nature, 475(7354), 59-64. https://doi.org/10.1038/nature10191

Vancouver

Gourdon PE, Liu X-Y, Skjørringe T, Morth JP, Møller LB, Pedersen BP et al. Crystal structure of a copper-transporting PIB-type ATPase. Nature. 2011 Jul 7;475(7354):59-64. https://doi.org/10.1038/nature10191

Author

Gourdon, Pontus Emanuel ; Liu, Xiang-Yu ; Skjørringe, Tina ; Morth, J Preben ; Møller, Lisbeth Birk ; Pedersen, Bjørn Panyella ; Nissen, Poul. / Crystal structure of a copper-transporting PIB-type ATPase. In: Nature. 2011 ; Vol. 475, No. 7354. pp. 59-64.

Bibtex

@article{364c5da4bed243789769203884f30a44,

title = "Crystal structure of a copper-transporting PIB-type ATPase",

abstract = "Heavy-metal homeostasis and detoxification is crucial for cell viability. P-type ATPases of the class IB (PIB) are essential in these processes, actively extruding heavy metals from the cytoplasm of cells. Here we present the structure of a PIB-ATPase, a Legionella pneumophila CopA Cu(+)-ATPase, in a copper-free form, as determined by X-ray crystallography at 3.2 {\AA} resolution. The structure indicates a three-stage copper transport pathway involving several conserved residues. A PIB-specific transmembrane helix kinks at a double-glycine motif displaying an amphipathic helix that lines a putative copper entry point at the intracellular interface. Comparisons to Ca(2+)-ATPase suggest an ATPase-coupled copper release mechanism from the binding sites in the membrane via an extracellular exit site. The structure also provides a framework to analyse missense mutations in the human ATP7A and ATP7B proteins associated with Menkes' and Wilson's diseases.",

keywords = "Adenosine Triphosphatases, Bacterial Proteins, Binding Sites, Biological Transport, Calcium, Cation Transport Proteins, Cell Membrane, Copper, Crystallography, X-Ray, Cytoplasm, Hepatolenticular Degeneration, Humans, Legionella pneumophila, Menkes Kinky Hair Syndrome, Models, Molecular, Mutation, Missense, Protein Structure, Tertiary, Sarcoplasmic Reticulum Calcium-Transporting ATPases, Structure-Activity Relationship",

author = "Gourdon, {Pontus Emanuel} and Xiang-Yu Liu and Tina Skj{\o}rringe and Morth, {J Preben} and M{\o}ller, {Lisbeth Birk} and Pedersen, {Bj{\o}rn Panyella} and Poul Nissen",

year = "2011",

month = jul,

day = "7",

doi = "10.1038/nature10191",

language = "English",

volume = "475",

pages = "59--64",

journal = "Nature",

issn = "0028-0836",

publisher = "nature publishing group",

number = "7354",

}

RIS

TY - JOUR

T1 - Crystal structure of a copper-transporting PIB-type ATPase

AU - Gourdon, Pontus Emanuel

AU - Liu, Xiang-Yu

AU - Skjørringe, Tina

AU - Morth, J Preben

AU - Møller, Lisbeth Birk

AU - Pedersen, Bjørn Panyella

AU - Nissen, Poul

PY - 2011/7/7

Y1 - 2011/7/7

N2 - Heavy-metal homeostasis and detoxification is crucial for cell viability. P-type ATPases of the class IB (PIB) are essential in these processes, actively extruding heavy metals from the cytoplasm of cells. Here we present the structure of a PIB-ATPase, a Legionella pneumophila CopA Cu(+)-ATPase, in a copper-free form, as determined by X-ray crystallography at 3.2 Å resolution. The structure indicates a three-stage copper transport pathway involving several conserved residues. A PIB-specific transmembrane helix kinks at a double-glycine motif displaying an amphipathic helix that lines a putative copper entry point at the intracellular interface. Comparisons to Ca(2+)-ATPase suggest an ATPase-coupled copper release mechanism from the binding sites in the membrane via an extracellular exit site. The structure also provides a framework to analyse missense mutations in the human ATP7A and ATP7B proteins associated with Menkes' and Wilson's diseases.

AB - Heavy-metal homeostasis and detoxification is crucial for cell viability. P-type ATPases of the class IB (PIB) are essential in these processes, actively extruding heavy metals from the cytoplasm of cells. Here we present the structure of a PIB-ATPase, a Legionella pneumophila CopA Cu(+)-ATPase, in a copper-free form, as determined by X-ray crystallography at 3.2 Å resolution. The structure indicates a three-stage copper transport pathway involving several conserved residues. A PIB-specific transmembrane helix kinks at a double-glycine motif displaying an amphipathic helix that lines a putative copper entry point at the intracellular interface. Comparisons to Ca(2+)-ATPase suggest an ATPase-coupled copper release mechanism from the binding sites in the membrane via an extracellular exit site. The structure also provides a framework to analyse missense mutations in the human ATP7A and ATP7B proteins associated with Menkes' and Wilson's diseases.

KW - Adenosine Triphosphatases

KW - Bacterial Proteins

KW - Binding Sites

KW - Biological Transport

KW - Calcium

KW - Cation Transport Proteins

KW - Cell Membrane

KW - Copper

KW - Crystallography, X-Ray

KW - Cytoplasm

KW - Hepatolenticular Degeneration

KW - Humans

KW - Legionella pneumophila

KW - Menkes Kinky Hair Syndrome

KW - Models, Molecular

KW - Mutation, Missense

KW - Protein Structure, Tertiary

KW - Sarcoplasmic Reticulum Calcium-Transporting ATPases

KW - Structure-Activity Relationship

U2 - 10.1038/nature10191

DO - 10.1038/nature10191

M3 - Journal article

C2 - 21716286

VL - 475

SP - 59

EP - 64

JO - Nature

JF - Nature

SN - 0028-0836

IS - 7354

ER -

ID: 126103702