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Open-and-shut cases in coiled-coil assembly: -sheets and -cylinders

Centre for Biomolecular Design and Drug Development, School of Biological Sciences, University of Sussex, Falmer BN1 9QG, UK

Reprint requests to: Derek Woolfson, School of Biological Sciences, University of Sussex, Falmer BN1 9QG, UK; e-mail: dek{at}biols.susx.ac.uk; fax: 44-1273-678433.

The coiled coil is a ubiquitous protein-folding motif. It generally is accepted that coiled coils are characterized by sequence patterns known as heptad repeats. Such patterns direct the formation and assembly of amphipathic -helices, the hydrophobic faces of which interface in a specific manner first proposed by Crick and termed "knobs-into-holes packing". We developed software, SOCKET, to recognize this packing in protein structures. As expected, in a trawl of the protein data bank, we found examples of canonical coiled coils with a single contiguous heptad repeat. In addition, we identified structures with multiple, overlapping heptad repeats. This observation extends Crick's original postulate: Multiple, offset heptad repeats help explain assemblies with more than two helices. Indeed, we have found that the sequence offset of the multiple heptad repeats is related to the coiled-coil oligomer state. Here we focus on one particular sequence motif in which two heptad repeats are offset by two residues. This offset sets up two hydrophobic faces separated by 150°–160° around the -helix. In turn, two different combinations of these faces are possible. Either similar or opposite faces can interface, which leads to open or closed multihelix assemblies. Accordingly, we refer to these two forms as -sheets and -cylinders. We illustrate these structures with our own predictions and by reference to natural variants on these designs that have recently come to light.

Keywords: -Cylinder; -sheet; amphipathic -helix; coiled coil; colicin Ia; knobs-into-holes packing; TolC; variant surface glycoproteins

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