1ysf
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= ABRB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | |GENE= ABRB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1yfb|1YFB]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ysf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ysf OCA], [http://www.ebi.ac.uk/pdbsum/1ysf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ysf RCSB]</span> | ||
}} | }} | ||
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[[Category: Djuranovic, S.]] | [[Category: Djuranovic, S.]] | ||
[[Category: Truffault, V.]] | [[Category: Truffault, V.]] | ||
| - | [[Category: | + | [[Category: bioinformatic]] |
| + | [[Category: homodimer]] | ||
| + | [[Category: nmr]] | ||
| + | [[Category: swapped-hairpin barrel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:20:28 2008'' |
Revision as of 22:20, 30 March 2008
| |||||||
| Gene: | ABRB (Bacillus subtilis) | ||||||
| Related: | 1YFB
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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