Home  |  Contact
PROSITE documentation PDOC51502

Stress-response A/B barrel domain profile





Description

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)


References

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
DOI10.1074/jbc.M409422200

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
DOI10.1023/B:JNMR.0000032525.70677.16

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
DOI10.1074/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 prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)