FEBS Letters
Volume 580, Issue 2 , Pages 358-362, 23 January 2006

Inverted repeat domains in membrane proteins

Edited by Sandro Sonnino

The Scripps Research Institute, Department of Molecular Biology, 10550 North Torrey Pines Road, CB-105, La Jolla, CA 92037, United States

Received 8 December 2005; accepted 19 December 2005. published online 05 January 2006.

Abstract 

With the upsurge in known membrane protein structures, common structural themes have started to emerge. One of these is the inverted repeat, a tandem of α-helical domains that have similar tertiary folds but opposite membrane orientations. In all previously known examples, both repeat units were encoded in a single continuous polypeptide. Recent structures of a bacterial multidrug transporter, EmrE, revealed an inverted repeat membrane protein wherein the two repeat units are assembled from two polypeptides with the same primary sequence. Here, we speculate on some of the implications of the EmrE structure with regards to our understanding of membrane protein evolution and topogenesis.

Keywords: Membrane protein structure, Evolution, Topology, Lipid, Membrane

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PII: S0014-5793(05)01537-1

doi:10.1016/j.febslet.2005.12.054

FEBS Letters
Volume 580, Issue 2 , Pages 358-362, 23 January 2006