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Exploring the allowed sequence space of a membrane protein

Nature Structural Biology volume 3, pages 141–148 (1996)Cite this article

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 reside 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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Authors and Affiliations

  1. Department of Chemistry and Biochemistry and UCLA-DOE Laboratory of Structural Biology and Molecular Medicine University of California, Los Angeles 405 Hilgard Av., Los Angeles, California, 90095-1570, USA

    Juan Wen, Xing Chen & James U. Bowie

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  1. Juan Wen
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  2. Xing Chen
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  3. James U. Bowie
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Wen, J., Chen, X. & Bowie, J. Exploring the allowed sequence space of a membrane protein. Nat Struct Mol Biol 3, 141–148 (1996). https://doi.org/10.1038/nsb0296-141

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