Journal
STRUCTURE
Volume 13, Issue 6, Pages 919-928Publisher
CELL PRESS
DOI: 10.1016/j.str.2005.03.017
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AbrB is a key transition-state regulator of Bacillus subtilis. Based on the conservation of a pup structural unit, we proposed a beta barrel fold for its DNA binding domain, similar to, but topologically distinct from, double-psi beta 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, PrIF, MraZ, addiction module antidotes (Pem1, MazE), plasmid maintenance proteins (VagC, VapB), and archaeal PhoU homologs. MazE and MraZ form swapped-hairpin beta 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 pup 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.
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