1ysf
From Proteopedia
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The solution structure of the N-domain of the transcription factor abrB
Overview
AbrB is a key transition-state regulator of Bacillus subtilis. Based on, the conservation of a betaalphabeta 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, PrlF, MraZ, addiction module antidotes (PemI, 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 betaalphabeta 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.
About this Structure
1YSF is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
AbrB-like transcription factors assume a swapped hairpin fold that is evolutionarily related to double-psi beta barrels., Coles M, Djuranovic S, Soding J, Frickey T, Koretke K, Truffault V, Martin J, Lupas AN, Structure. 2005 Jun;13(6):919-28. PMID:15939023
Page seeded by OCA on Wed Nov 21 07:01:23 2007
