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Inverted repeat domains in membrane proteins.

Owen Pornillos1, Geoffrey Chang

  • 1The Scripps Research Institute, Department of Molecular Biology, La Jolla, CA 92037, USA.

FEBS Letters
|January 13, 2006
PubMed
Summary
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The bacterial multidrug transporter EmrE features an inverted repeat structure assembled from two identical polypeptides. This finding challenges previous models of membrane protein assembly and evolution.

Area of Science:

  • Structural Biology
  • Membrane Protein Research
  • Biochemistry

Background:

  • Membrane proteins exhibit common structural motifs, including inverted repeats.
  • Previously, inverted repeat units were exclusively found within single polypeptide chains.

Purpose of the Study:

  • To investigate the structural implications of the bacterial multidrug transporter EmrE.
  • To explore the evolutionary and topogenesis aspects of membrane proteins based on EmrE structure.

Main Methods:

  • Analysis of recent structural data for the EmrE transporter.
  • Comparative structural analysis of known membrane proteins.

Main Results:

  • EmrE exhibits an inverted repeat structure.

Related Experiment Videos

  • Unlike prior examples, EmrE's repeat units are derived from two polypeptides with identical primary sequences.

    • Conclusions:

    • The EmrE structure provides a novel paradigm for membrane protein assembly.
    • This finding necessitates a re-evaluation of membrane protein evolution and topogenesis models.