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          Institute: MPI für Entwicklungsbiologie     Collection: Abteilung 1 - Protein Evolution (A. Lupas)     Display Documents



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ID: 246115.0, MPI für Entwicklungsbiologie / Abteilung 1 - Protein Evolution (A. Lupas)
AbrB-like transcription factors assume a swapped hairpin fold that is evolutionarily related to double-psi beta barrels.
Authors:Coles, Murray; Djuranovic, Sergeij; Soeding, Johannes; Frickey, Tankred; Koretke, K; Truffault, V; Martin, Joerg; Lupas, Andrei
Language:English
Date of Publication (YYYY-MM-DD):2005-06
Title of Journal:Structure (Camb).
Volume:13
Issue / Number:6
Start Page:919
End Page:928
Sequence Number of Article:15939023
Review Status:not specified
Audience:Experts Only
Abstract / Description: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.
External Publication Status:published
Document Type:Article
Affiliations:MPI für Entwicklungsbiologie/Abteilung 1 - Proteinevolution (Andrei Lupas)
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