Exploring the allowed sequence space of a membrane protein.
We present a comprehensive view of the tolerance of a membrane protein to sequence substitution. We find that the protein, diacylglycerol kinase from Escherichia coli, is extremely tolerant to sequence changes with three-quarters of the residues tolerating non-conservative changes. The conserved residues are distributed with approximately the same frequency in the soluble and transmembrane portions of the protein, but the most critical active-site residues appear to residue in the second cytoplasmic domain. It is remarkable that a unique structure of the membrane embedded portion of the protein can be encoded by a sequence that is so tolerant to substitution.
Wen
J
J
Department of Chemistry and Biochemistry, University of California, Los Angeles 90095-1570, USA.
Chen
X
X
Bowie
J U
JU
D000595:Amino Acid Sequence; D001665:Binding Sites / Q000235:genetics; D003198:Computer Simulation; D017124:Conserved Sequence / Q000235:genetics*; D019852:Diacylglycerol Kinase; D004926:Escherichia coli / Q000201:enzymology; D008969:Molecular Sequence Data; D016296:Mutagenesis; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000737:chemistry* / Q000235:genetics; D017434:Protein Structure, Tertiary
D017853:Phosphotransferases (Alcohol Group Acceptor); D019852:Diacylglycerol Kinase