PROSITE documentation PDOC51502
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 α+β barrels in which the two β-sheets form a β-barrel. The two molecules in the dimer are related by a 2-fold axis parallel to helix H1 and β-strands B3 and B4. The outer surface of the β-sheets of the two molecules forms a β-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 α/β structure consisting of a four-stranded antiparallel β-sheet and three α-helices, arranged in a β-α-β-β-α-α-β topology (see <PDB:1Q4R>). Two sheets join at their edges to form an oblong β-barrel, flanked by four helices on each of the opposing faces. C-terminal residues extending from the β4 strand of each monomer wrap around and connect with the β2 strand and α1 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.

Last update:

August 2010 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

S_R_A_B_BARREL, PS51502; Stress-response A/B barrel domain profile  (MATRIX)


1AuthorsLytle B.L. Peterson F.C. Qiu S.H. Luo M. Zhao Q. Markley J.L. Volkman B.F.
TitleSolution structure of a ubiquitin-like domain from tubulin-binding cofactor B.
SourceJ. Biol. Chem. 279:46787-46793(2004).
PubMed ID15364906

2AuthorsCornilescu G. Cornilescu C.C. Zhao Q. Frederick R.O. Peterson F.C. Thao S. Markley J.L.
TitleSolution structure of a homodimeric hypothetical protein, At5g22580, a structural genomics target from Arabidopsis thaliana.
SourceJ. Biomol. NMR 29:387-390(2004).
PubMed ID15213437

3AuthorsDgany O. Gonzalez A. Sofer O. Wang W. Zolotnitsky G. Wolf A. Shoham Y. Altman A. Wolf S.G. Shoseyov O. Almog O.
TitleThe structural basis of the thermostability of SP1, a novel plant (Populus tremula) boiling stable protein.
SourceJ. Biol. Chem. 279:51516-51523(2004).
PubMed ID15371455

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