Format

Send to

Choose Destination
See comment in PubMed Commons below
J Biochem. 1998 Dec 1;124(6):1051-9.

Structures of membrane proteins determined at atomic resolution.

Author information

1
Institute for Protein Research, Osaka University, Suita, Osaka, 565-0871, Japan.

Abstract

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 A 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 beta-strand. The central +10 A region of the transmembrane alpha-helix is dominated by hydrophobic residues. On both sides of the central region are concentrated polar aromatic residues. Charged residues are dominant around +15 A to +20 A. All the transmembrane beta-structures are found in pore-forming proteins. The central region of the transmembrane beta-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 beta-structure is similar to that of the transmembrane alpha-helix. alpha-Helices anchoring the membrane surface region are amphipathic with hydrophobic residues inside and hydrophilic residues outside.

PMID:
9832606
[Indexed for MEDLINE]
Free full text
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for J-STAGE, Japan Science and Technology Information Aggregator, Electronic
    Loading ...
    Support Center