Exploring the allowed sequence space of a membrane protein.

J Wen; X Chen; J U Bowie

doi:10.1038/nsb0296-141

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Exploring the allowed sequence space of a membrane protein.

J Wen·X Chen·J U Bowie

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Abstract

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.

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Amino Acid Sequence Binding Sites Computer Simulation Conserved Sequence Diacylglycerol Kinase Escherichia coli Molecular Sequence Data Mutagenesis Phosphotransferases (Alcohol Group Acceptor)Protein Structure, Tertiary Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

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J Wen, X Chen, J U Bowie. 1996. Exploring the allowed sequence space of a membrane protein.. https://doi.org/10.1038/nsb0296-141

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