Internally bridging water molecule in transmembrane α-helical kink

There are hundreds of membrane protein atomic coordinates in the Protein Data Bank (PDB), and high-resolution structures of better than 2.5 Å enable the visualization of a sizable number of amphiphiles (lipid and/or detergent) and bound water molecules as essential parts of the structure. Upon scrut...

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Bibliographic Details
Published in:Current opinion in structural biology 2010-08, Vol.20 (4), p.456-463
Main Authors: Miyano, Masashi, Ago, Hideo, Saino, Hiromichi, Hori, Tetsuya, Ida, Koh
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Cell Membrane
Humans
Membrane Proteins - chemistry
Membrane Proteins - metabolism
Molecular Sequence Data
Protein Structure, Secondary
Water - chemistry
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Summary:There are hundreds of membrane protein atomic coordinates in the Protein Data Bank (PDB), and high-resolution structures of better than 2.5 Å enable the visualization of a sizable number of amphiphiles (lipid and/or detergent) and bound water molecules as essential parts of the structure. Upon scrutinizing these high-resolution structures, water molecules were found to ‘wedge’ and stabilize large kink angle (30–40°) in a simple cylindrical model at the transmembrane helical kinks so as to form an inter-helical cavity to accommodate a ligand binding or active site as a crucial structural feature in α-helical integral membrane proteins. Furthermore, some of these water molecules are proposed to play a pivotal role of their conformational change to exert their functional regulation.
ISSN:0959-440X
1879-033X
DOI:10.1016/j.sbi.2010.05.008