Structure of the reaction center from Rhodobacter sphaeroides R-26: membrane-protein interactions.

T. O. Yeates, H. Komiya, D. C. Rees, James Paul Allen, G. Feher

Research output: Contribution to journalArticle

196 Citations (Scopus)

Abstract

The energetics of membrane-protein interactions are analyzed with the three-dimensional model of the photosynthetic reaction center (RC) from Rhodobacter sphaeroides. The position of the RC in the membrane and the thickness of the membrane were obtained by minimizing the hydrophobic energy with the energy function of Eisenberg and McLachlan. The 2-fold symmetry axis that relates the L and M subunits is, within the accuracy of 5 degrees, parallel to the normal of the membrane. The thickness of the membrane is estimated to be 40-45 A. Residues that are exposed to the membrane are relatively poorly conserved in the sequences of homologous RC proteins. The surface area of the RC is comparable to the surface areas of water-soluble proteins of similar molecular weight. The volumes of interior atoms in the RC are also similar to those of water-soluble proteins, indicating the same compact packing for both types of proteins. The electrostatic potential of the cofactors was calculated. The results show an asymmetry in the potential between the two possible pathways of electron transfer, with the A branch being preferred electrostatically.

Original languageEnglish
Pages (from-to)6438-6442
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume84
Issue number18
Publication statusPublished - Sep 1987

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Rhodobacter sphaeroides
Membrane Proteins
Membranes
Proteins
Photosynthetic Reaction Center Complex Proteins
Water
Conserved Sequence
Static Electricity
Molecular Weight
Electrons

ASJC Scopus subject areas

  • General
  • Genetics

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Structure of the reaction center from Rhodobacter sphaeroides R-26 : membrane-protein interactions. / Yeates, T. O.; Komiya, H.; Rees, D. C.; Allen, James Paul; Feher, G.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 84, No. 18, 09.1987, p. 6438-6442.

Research output: Contribution to journalArticle

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N2 - The energetics of membrane-protein interactions are analyzed with the three-dimensional model of the photosynthetic reaction center (RC) from Rhodobacter sphaeroides. The position of the RC in the membrane and the thickness of the membrane were obtained by minimizing the hydrophobic energy with the energy function of Eisenberg and McLachlan. The 2-fold symmetry axis that relates the L and M subunits is, within the accuracy of 5 degrees, parallel to the normal of the membrane. The thickness of the membrane is estimated to be 40-45 A. Residues that are exposed to the membrane are relatively poorly conserved in the sequences of homologous RC proteins. The surface area of the RC is comparable to the surface areas of water-soluble proteins of similar molecular weight. The volumes of interior atoms in the RC are also similar to those of water-soluble proteins, indicating the same compact packing for both types of proteins. The electrostatic potential of the cofactors was calculated. The results show an asymmetry in the potential between the two possible pathways of electron transfer, with the A branch being preferred electrostatically.

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