Journal Article

Structures of Membrane Proteins Determined at Atomic Resolution

Hiroaki Sakai and Tomitake Tsukihara

in The Journal of Biochemistry

Published on behalf of The Japanese Biochemical Society

Volume 124, issue 5, pages 1051-1059
Published in print November 1998 | ISSN: 0021-924X
Published online November 1998 | e-ISSN: 1756-2651 | DOI: https://dx.doi.org/10.1093/oxfordjournals.jbchem.a022199
Structures of Membrane Proteins Determined at Atomic Resolution

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Following determination of the first crystal structure of the reaction center of Rhodopseudomonas viridis, a membrane protein, by X-ray crystal structure analysis at 3.0 A resolution, 18 X-ray crystal structures and two electron crystal structures of membrane proteins have been obtained at higher than 3.5 Å resolution. Besides these integral membrane protein structures, three crystal structures of water-soluble proteins, which can enter membranes, have been determined by X-ray crystallography at high resolution. The structural features of membrane proteins have been summarized by inspecting these crystal structures. The polypeptide chain crosses the membrane in a helical conformation or a β-strand. The central +10 Å region of the transmembrane α-helix is dominated by hydrophobic residues. On both sides of the central region are concentrated polar aromatic residues. Charged residues are dominant around +15 Å to +20 Å. All the transmembrane β-structures are found in pore-forming proteins. The central region of the transmembrane β-structure is amphipathic with hydrophobic residues on the membrane exposed side. The distribution of amino acid residues on the membrane exposed surface of the transmembrane β-structure is similar to that of the transmembrane α-helix. α-Helices anchoring the membrane surface region are amphipathic with hydrophobic residues inside and hydrophilic residues outside.

Keywords: membrane protein; X-ray crystal structure analysis

Journal Article.  0 words. 

Subjects: Biochemistry

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