ATP synthase: structure-function relationships

Philip J. Thomas; Mario Bianchet; David N. Garboczi; Joanne Hullihen; L. Mario Amzel; Peter L. Pedersen

doi:10.1016/S0005-2728(05)80027-1

ATP synthase: structure-function relationships

Philip J. Thomas, Mario Bianchet, David N. Garboczi, Joanne Hullihen, L. Mario Amzel, Peter L. Pedersen

School of Medicine

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

Abstract

Recent work has focused on obtaining a better understanding of the three-dimensional structural relationships between the α and β subunits of the F₁ moiety and the location of nucleotide binding domains within these subunits. Four types of approach are currently being pursued: X-ray crystallographic, chemical, molecular biological and biochemical. Here we briefly review some of the major conclusions of these studies, and point out some of the problems that must be resolved before an adequate model that relates structure to function in the ATP synthase molecule can be formulated.

Original language	English (US)
Pages (from-to)	228-231
Number of pages	4
Journal	Biochimica et Biophysica Acta - Bioenergetics
Volume	1101
Issue number	2
DOIs	https://doi.org/10.1016/S0005-2728(05)80027-1
State	Published - 1992

Keywords

ATP synthase
ATP synthesis
ATPase, F-

ASJC Scopus subject areas

Biophysics
Biochemistry
Cell Biology

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10.1016/S0005-2728(05)80027-1

Cite this

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title = "ATP synthase: structure-function relationships",

abstract = "Recent work has focused on obtaining a better understanding of the three-dimensional structural relationships between the α and β subunits of the F1 moiety and the location of nucleotide binding domains within these subunits. Four types of approach are currently being pursued: X-ray crystallographic, chemical, molecular biological and biochemical. Here we briefly review some of the major conclusions of these studies, and point out some of the problems that must be resolved before an adequate model that relates structure to function in the ATP synthase molecule can be formulated.",

keywords = "ATP synthase, ATP synthesis, ATPase, F-",

author = "Thomas, {Philip J.} and Mario Bianchet and Garboczi, {David N.} and Joanne Hullihen and Amzel, {L. Mario} and Pedersen, {Peter L.}",

note = "Funding Information: This work was supported by NIH grant CA 10951 to P.L.P. and by NIH Grant GM 25432 to L.M.A.",

year = "1992",

doi = "10.1016/S0005-2728(05)80027-1",

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T1 - ATP synthase

T2 - structure-function relationships

AU - Thomas, Philip J.

AU - Bianchet, Mario

AU - Garboczi, David N.

AU - Hullihen, Joanne

AU - Amzel, L. Mario

AU - Pedersen, Peter L.

N1 - Funding Information: This work was supported by NIH grant CA 10951 to P.L.P. and by NIH Grant GM 25432 to L.M.A.

PY - 1992

Y1 - 1992

N2 - Recent work has focused on obtaining a better understanding of the three-dimensional structural relationships between the α and β subunits of the F1 moiety and the location of nucleotide binding domains within these subunits. Four types of approach are currently being pursued: X-ray crystallographic, chemical, molecular biological and biochemical. Here we briefly review some of the major conclusions of these studies, and point out some of the problems that must be resolved before an adequate model that relates structure to function in the ATP synthase molecule can be formulated.

AB - Recent work has focused on obtaining a better understanding of the three-dimensional structural relationships between the α and β subunits of the F1 moiety and the location of nucleotide binding domains within these subunits. Four types of approach are currently being pursued: X-ray crystallographic, chemical, molecular biological and biochemical. Here we briefly review some of the major conclusions of these studies, and point out some of the problems that must be resolved before an adequate model that relates structure to function in the ATP synthase molecule can be formulated.

KW - ATP synthase

KW - ATP synthesis

KW - ATPase, F-

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ATP synthase: structure-function relationships

Abstract

Keywords

ASJC Scopus subject areas

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