{PDOC51502} {PS51502; S_R_A_B_BARREL} {BEGIN} ********************************************* * Stress-response A/B barrel domain profile * ********************************************* The stress-response A/B barrel domain is found in a class of stress-response proteins in plants and in some bacterial fructose-bisphosphate aldolase. 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 two beta-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. 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 [1,2,3]. The stress-response A/B barrel domain has an alpha/beta structure consisting of a four-stranded antiparallel beta-sheet and three alpha-helices, arranged in a Beta-Alpha-Beta-Beta-Alpha-Alpha-Beta topology (see ). Two sheets join at their edges to form an oblong beta-barrel, flanked by four helices on each of the opposing faces. 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 [1,2,3]. 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) (also known as Pop3 in other Populus species), a thermostable stress-responsive protein. - Pseudomonas hydrogenothermophila fructose 1,6-bisphosphate aldolase (cbbA). The profile we developed covers the entire stress-response A/B barrel domain. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: August 2010 / First entry. [ 1] Lytle B.L., Peterson F.C., Qiu S.H., Luo M., Zhao Q., Markley J.L., Volkman B.F. "Solution structure of a ubiquitin-like domain from tubulin-binding cofactor B." J. Biol. Chem. 279:46787-46793(2004). PubMed=15364906; DOI=10.1074/jbc.M409422200 [ 2] Cornilescu G., Cornilescu C.C., Zhao Q., Frederick R.O., Peterson F.C., Thao S., Markley J.L. "Solution structure of a homodimeric hypothetical protein, At5g22580, a structural genomics target from Arabidopsis thaliana." J. Biomol. NMR 29:387-390(2004). PubMed=15213437; DOI=10.1023/B:JNMR.0000032525.70677.16 [ 3] Dgany O., Gonzalez A., Sofer O., Wang W., Zolotnitsky G., Wolf A., Shoham Y., Altman A., Wolf S.G., Shoseyov O., Almog O. "The structural basis of the thermostability of SP1, a novel plant (Populus tremula) boiling stable protein." J. Biol. Chem. 279:51516-51523(2004). PubMed=15371455; DOI=10.1074/jbc.M409952200 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}