Cytochrome oxidase: structural insights from electron microscopy and from secondary structure prediction

Terrence G. Frey; Leslie A. Kuhn; John S. Leigh; M. J. Costello; Samuel H.P. Chan

doi:10.1016/0162-0134(85)85020-0

Cytochrome oxidase: structural insights from electron microscopy and from secondary structure prediction

Terrence G. Frey, Leslie A. Kuhn, John S. Leigh, M. J. Costello, Samuel H.P. Chan

Department of Biology

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

9 Scopus citations

Abstract

Electron microscopic images of selectively contrasted cytochrome oxidase dimer crystals are interpreted in a manner consistent with the structure of monomers determined by Fuller et al. (J. Molec. Biol. 134, 305-327). The arms of the y-shaped monomers lie within and perpendicular to the lipid bilayer protruding approximately 25 Å on the matrix side of the membrane. The cytoplasmic-side tails of two monomers spread apart in a dimer forming a large cleft. Decoration of the exposed matrix side of vesicle crystals with antisubunit IV antibody fragments indicates that subunit IV lies along the a-crystal axis roughly 20 Å from the center of the dimer. A membrane propensity algorithm applied to the sequences of cytochrome oxidase subunits predicts a total of 19 transmembrane α-helices per monomer.

Original language	English (US)
Pages (from-to)	155-162
Number of pages	8
Journal	Journal of Inorganic Biochemistry
Volume	23
Issue number	3-4
DOIs	https://doi.org/10.1016/0162-0134(85)85020-0
State	Published - 1985

ASJC Scopus subject areas

Biochemistry
Inorganic Chemistry

Access to Document

10.1016/0162-0134(85)85020-0

Cite this

@article{15ed023621e04ff88fe7c9520010937a,

title = "Cytochrome oxidase: structural insights from electron microscopy and from secondary structure prediction",

abstract = "Electron microscopic images of selectively contrasted cytochrome oxidase dimer crystals are interpreted in a manner consistent with the structure of monomers determined by Fuller et al. (J. Molec. Biol. 134, 305-327). The arms of the y-shaped monomers lie within and perpendicular to the lipid bilayer protruding approximately 25 {\AA} on the matrix side of the membrane. The cytoplasmic-side tails of two monomers spread apart in a dimer forming a large cleft. Decoration of the exposed matrix side of vesicle crystals with antisubunit IV antibody fragments indicates that subunit IV lies along the a-crystal axis roughly 20 {\AA} from the center of the dimer. A membrane propensity algorithm applied to the sequences of cytochrome oxidase subunits predicts a total of 19 transmembrane α-helices per monomer.",

author = "Frey, {Terrence G.} and Kuhn, {Leslie A.} and Leigh, {John S.} and Costello, {M. J.} and Chan, {Samuel H.P.}",

note = "Funding Information: This work was supported by the following grants from the National Institutes of Health : GM-28750 T.G.F. GM-25052 J.S.L. RRO-1747 GM-27914 M.J.C. and CA-20454 S.H. P . C. .",

year = "1985",

doi = "10.1016/0162-0134(85)85020-0",

language = "English (US)",

volume = "23",

pages = "155--162",

journal = "Journal of Inorganic Biochemistry",

issn = "0162-0134",

publisher = "Elsevier",

number = "3-4",

}

TY - JOUR

T1 - Cytochrome oxidase

T2 - structural insights from electron microscopy and from secondary structure prediction

AU - Frey, Terrence G.

AU - Kuhn, Leslie A.

AU - Leigh, John S.

AU - Costello, M. J.

AU - Chan, Samuel H.P.

N1 - Funding Information: This work was supported by the following grants from the National Institutes of Health : GM-28750 T.G.F. GM-25052 J.S.L. RRO-1747 GM-27914 M.J.C. and CA-20454 S.H. P . C. .

PY - 1985

Y1 - 1985

N2 - Electron microscopic images of selectively contrasted cytochrome oxidase dimer crystals are interpreted in a manner consistent with the structure of monomers determined by Fuller et al. (J. Molec. Biol. 134, 305-327). The arms of the y-shaped monomers lie within and perpendicular to the lipid bilayer protruding approximately 25 Å on the matrix side of the membrane. The cytoplasmic-side tails of two monomers spread apart in a dimer forming a large cleft. Decoration of the exposed matrix side of vesicle crystals with antisubunit IV antibody fragments indicates that subunit IV lies along the a-crystal axis roughly 20 Å from the center of the dimer. A membrane propensity algorithm applied to the sequences of cytochrome oxidase subunits predicts a total of 19 transmembrane α-helices per monomer.

AB - Electron microscopic images of selectively contrasted cytochrome oxidase dimer crystals are interpreted in a manner consistent with the structure of monomers determined by Fuller et al. (J. Molec. Biol. 134, 305-327). The arms of the y-shaped monomers lie within and perpendicular to the lipid bilayer protruding approximately 25 Å on the matrix side of the membrane. The cytoplasmic-side tails of two monomers spread apart in a dimer forming a large cleft. Decoration of the exposed matrix side of vesicle crystals with antisubunit IV antibody fragments indicates that subunit IV lies along the a-crystal axis roughly 20 Å from the center of the dimer. A membrane propensity algorithm applied to the sequences of cytochrome oxidase subunits predicts a total of 19 transmembrane α-helices per monomer.

UR - http://www.scopus.com/inward/record.url?scp=0022036203&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0022036203&partnerID=8YFLogxK

U2 - 10.1016/0162-0134(85)85020-0

DO - 10.1016/0162-0134(85)85020-0

M3 - Article

C2 - 2991452

AN - SCOPUS:0022036203

SN - 0162-0134

VL - 23

SP - 155

EP - 162

JO - Journal of Inorganic Biochemistry

JF - Journal of Inorganic Biochemistry

IS - 3-4

ER -

Cytochrome oxidase: structural insights from electron microscopy and from secondary structure prediction

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this