| Type: | Domain | Name: | Stress responsive alpha-beta barrel |
| Description: | The stress-response A/B barrel domain is found in a class of stress-response proteins in plants. It is also found in some bacterial fructose-bisphosphate aldolase such as at the C terminus of a fructose 1,6-bisphosphate aldolase from Hydrogenophilus thermoluteolus () []. is found in the pA01 plasmid, which encodes genes for molybdopterin uptake and degradation of plant alkaloid nicotine.The stress-response A/B barrel domain forms a very stable dimer. This dimer belongs to the superfamily of dimeric alpha+beta barrels in which the twobeta-sheets form a beta-barrel. The two molecules in the dimer are related by a 2-fold axis parallel to helix H1 and beta-strands B3 and B4. C-terminal residues extending from the beta4 strand of each monomer wrap around and connect with the beta2 strand and alpha1 helix of the opposing monomer to form the dimer interface [, , ].The outer surface of the beta-sheets of the two molecules forms a beta-barrel-like structure defining a central pore.The function of the stress-response A/B barrel domain is unknown [, , ], but it is upregulated in response to salt stress in Populus balsamifera(balsam poplar) [].Some proteins known to contain a stress response A/B barrel domain are listed below:- Arabidopsis thaliana At3g17210- Arabidopsis thaliana At5g22580-Populus tremula stable protein 1 (SP-1)(Populus species), a thermostable stress-responsive protein.- Pseudomonas hydrogenothermophila fructose 1,6-bisphosphate aldolase (cbbA).The structure of one of these proteins has been solved () and the domain forms an alpha-beta barrel dimer []. | Short Name: | Dabb |
