AbrB-like transcription factors assume a swapped hairpin fold that is 
evolutionarily related to double-psi beta barrels.

Coles, M.; Djuranovic, S.; Söding, J.; Frickey, T.; Koretke, K.; Truffault, V.; Martin, J.; Lupas, A. N.

doi:10.1016/j.str.2005.03.017

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AbrB-like transcription factors assume a swapped hairpin fold that is evolutionarily related to double-psi beta barrels.

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Söding, J.
Research Group of Computational Biology, MPI for Biophysical Chemistry, Max Planck Society;

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http://www.sciencedirect.com/science/article/pii/S0969212605001693/pdfft?md5=3f97b52ecd6fdbc6f1a1595d0b064242&pid=1-s2.0-S0969212605001693-main.pdf
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Citation

Coles, M., Djuranovic, S., Söding, J., Frickey, T., Koretke, K., Truffault, V., et al. (2005). AbrB-like transcription factors assume a swapped hairpin fold that is evolutionarily related to double-psi beta barrels. Structure, 13(6), 919-928. doi:10.1016/j.str.2005.03.017.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0017-EBDE-8

Abstract

AbrB is a key transition-state regulator of Bacillus subtilis. Based on the conservation of a βαβ structural unit, we proposed a β barrel fold for its DNA binding domain, similar to, but topologically distinct from, double-psi β barrels. However, the NMR structure revealed a novel fold, the “looped-hinge helix.” To understand this discrepancy, we undertook a bioinformatics study of AbrB and its homologs; these form a large superfamily, which includes SpoVT, PrlF, MraZ, addiction module antidotes (PemI, MazE), plasmid maintenance proteins (VagC, VapB), and archaeal PhoU homologs. MazE and MraZ form swapped-hairpin β barrels. We therefore reexamined the fold of AbrB by NMR spectroscopy and found that it also forms a swapped-hairpin barrel. The conservation of the core βαβ element supports a common evolutionary origin for swapped-hairpin and double-psi barrels, which we group into a higher-order class, the cradle-loop barrels, based on the peculiar shape of their ligand binding site.