TY - JOUR
T1 - Selectivity changes in site-directed mutants of the VDAC ion channel
T2 - Structural implications
AU - Blachly-Dyson, Elizabeth
AU - Peng, Songzhi
AU - Colombini, Marco
AU - Forte, Michael
PY - 1990
Y1 - 1990
N2 - The gene encoding the yeast mitochondrial outer membrane channel VDAC was subjected to site-directed mutagenesis to change amino acids at 29 positions to residues differing in charge from the wild-type sequence. The mutant genes were then expressed in yeast, and the physiological consequences of single and multiple amino acid changes were assessed after isolation and insertion of mutant channels into phospholipid bilayers. Selectivity changes were observed at 14 sites distributed throughout the length of the molecule. These sites are likely to define the position of the protein walls lining the aqueous pore and hence, the transmembrane segments. These results have been used to develop a model of the open state of the channel in which each polypeptide contributes 12 β strands and one a helix to form the aqueous transmembrane pathway.
AB - The gene encoding the yeast mitochondrial outer membrane channel VDAC was subjected to site-directed mutagenesis to change amino acids at 29 positions to residues differing in charge from the wild-type sequence. The mutant genes were then expressed in yeast, and the physiological consequences of single and multiple amino acid changes were assessed after isolation and insertion of mutant channels into phospholipid bilayers. Selectivity changes were observed at 14 sites distributed throughout the length of the molecule. These sites are likely to define the position of the protein walls lining the aqueous pore and hence, the transmembrane segments. These results have been used to develop a model of the open state of the channel in which each polypeptide contributes 12 β strands and one a helix to form the aqueous transmembrane pathway.
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U2 - 10.1126/science.1690454
DO - 10.1126/science.1690454
M3 - Article
C2 - 1690454
AN - SCOPUS:0025355620
SN - 0036-8075
VL - 247
SP - 1233
EP - 1236
JO - Science
JF - Science
IS - 4947
ER -