Molecular architecture of the copper-transporting ATPase ATP7B

Svetlana Lutsenko; Samuel Jayakanthan; Oleg Y. Dmitriev

doi:10.1016/B978-0-12-810532-0.00005-7

Molecular architecture of the copper-transporting ATPase ATP7B

Svetlana Lutsenko, Samuel Jayakanthan, Oleg Y. Dmitriev

School of Medicine

Research output: Chapter in Book/Report/Conference proceeding › Chapter

1 Scopus citations

Abstract

The copper-transporting ATPase ATP7B (Wilson ATPase) is a large trans-membrane protein with a complex multidomain architecture. ATP7B uses the subset of these domains to hydrolyze adenosine triphosphate (ATP) and to couple ATP hydrolysis with the transport of copper across the cell membranes. These activities are central to main physiological functions of ATP7B: the maintenance of copper homeostasis and synthesis of active ceruloplasmin. The other domains of ATP7B are used for regulation: using these structural elements, ATP7B responds to changing copper concentration in the cytoplasm and other signaling events. In this review, we summarize the available structural information on ATP7B and relate, whenever possible, the structural features of ATP7B to its function and regulation.

Original language	English (US)
Title of host publication	Clinical and Translational Perspectives on WILSON DISEASE
Publisher	Elsevier
Pages	33-43
Number of pages	11
ISBN (Electronic)	9780128105320
ISBN (Print)	9780128105337
DOIs	https://doi.org/10.1016/B978-0-12-810532-0.00005-7
State	Published - Jan 1 2018

Keywords

A domain
ATP7B structure
Metal-binding domains
N domain
Nuclear magnetic resonance spectroscopy (NMR spectroscopy)
P domain

ASJC Scopus subject areas

Medicine(all)

Access to Document

10.1016/B978-0-12-810532-0.00005-7

Cite this

@inbook{f3ccf030af1c4fa899814285a808e458,

title = "Molecular architecture of the copper-transporting ATPase ATP7B",

abstract = "The copper-transporting ATPase ATP7B (Wilson ATPase) is a large trans-membrane protein with a complex multidomain architecture. ATP7B uses the subset of these domains to hydrolyze adenosine triphosphate (ATP) and to couple ATP hydrolysis with the transport of copper across the cell membranes. These activities are central to main physiological functions of ATP7B: the maintenance of copper homeostasis and synthesis of active ceruloplasmin. The other domains of ATP7B are used for regulation: using these structural elements, ATP7B responds to changing copper concentration in the cytoplasm and other signaling events. In this review, we summarize the available structural information on ATP7B and relate, whenever possible, the structural features of ATP7B to its function and regulation.",

keywords = "A domain, ATP7B structure, Metal-binding domains, N domain, Nuclear magnetic resonance spectroscopy (NMR spectroscopy), P domain",

author = "Svetlana Lutsenko and Samuel Jayakanthan and Dmitriev, {Oleg Y.}",

year = "2018",

month = jan,

day = "1",

doi = "10.1016/B978-0-12-810532-0.00005-7",

language = "English (US)",

isbn = "9780128105337",

pages = "33--43",

booktitle = "Clinical and Translational Perspectives on WILSON DISEASE",

publisher = "Elsevier",

}

TY - CHAP

T1 - Molecular architecture of the copper-transporting ATPase ATP7B

AU - Lutsenko, Svetlana

AU - Jayakanthan, Samuel

AU - Dmitriev, Oleg Y.

PY - 2018/1/1

Y1 - 2018/1/1

N2 - The copper-transporting ATPase ATP7B (Wilson ATPase) is a large trans-membrane protein with a complex multidomain architecture. ATP7B uses the subset of these domains to hydrolyze adenosine triphosphate (ATP) and to couple ATP hydrolysis with the transport of copper across the cell membranes. These activities are central to main physiological functions of ATP7B: the maintenance of copper homeostasis and synthesis of active ceruloplasmin. The other domains of ATP7B are used for regulation: using these structural elements, ATP7B responds to changing copper concentration in the cytoplasm and other signaling events. In this review, we summarize the available structural information on ATP7B and relate, whenever possible, the structural features of ATP7B to its function and regulation.

AB - The copper-transporting ATPase ATP7B (Wilson ATPase) is a large trans-membrane protein with a complex multidomain architecture. ATP7B uses the subset of these domains to hydrolyze adenosine triphosphate (ATP) and to couple ATP hydrolysis with the transport of copper across the cell membranes. These activities are central to main physiological functions of ATP7B: the maintenance of copper homeostasis and synthesis of active ceruloplasmin. The other domains of ATP7B are used for regulation: using these structural elements, ATP7B responds to changing copper concentration in the cytoplasm and other signaling events. In this review, we summarize the available structural information on ATP7B and relate, whenever possible, the structural features of ATP7B to its function and regulation.

KW - A domain

KW - ATP7B structure

KW - Metal-binding domains

KW - N domain

KW - Nuclear magnetic resonance spectroscopy (NMR spectroscopy)

KW - P domain

UR - http://www.scopus.com/inward/record.url?scp=85092555635&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85092555635&partnerID=8YFLogxK

U2 - 10.1016/B978-0-12-810532-0.00005-7

DO - 10.1016/B978-0-12-810532-0.00005-7

M3 - Chapter

AN - SCOPUS:85092555635

SN - 9780128105337

SP - 33

EP - 43

BT - Clinical and Translational Perspectives on WILSON DISEASE

PB - Elsevier

ER -

Molecular architecture of the copper-transporting ATPase ATP7B

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this