Dim A B barrel

Dimeric alpha beta barrel domain
Cartoon representation of the molecular structure of the Crystal structure of the protein from gene At3g17210 of Arabidopsis thaliana (PDB: 1q4r​)[1]
Identifiers
SymbolDim_A_B_barrel
Pfam clanCL0032
ECOD304.4
InterProIPR011008
Available protein structures:
PDB  IPR011008  
AlphaFold

In molecular biology dimeric alpha beta barrel domain (Dim_A_B_barrel) is a protein structural motif found in proteins with a ferredoxin-like fold.[2]

Structure

Pairs of these proteins assemble into a beta barrel structure.[3] Dimeric α-β barrel domains exhibit an α+β sandwich fold with an antiparallel β-sheet that forms a closed barrel. These domains dimerise through the β-sheet, and in some cases these dimers may assemble into higher oligomers.[4]

Function

The function of this barrel is quite varied, indicating versatility in its biological roles.[3]

Examples

Domains with this structure are found in proteins from several different families,[5] including:

  • Bacterial actinorhodin biosynthesis monooxygenase (ActVa-Orf6), which catalyses the oxidation of an aromatic intermediate of the actinorhodin biosynthetic pathway[6]
  • Bacterial muconalactone isomerase, a decamer composed of five dimers[7]
  • The C-terminal domain of archaeal LprA, a member of the Lrp/AqsnC family of transcription regulators[8]

References

  1. ↑ Bingman CA, Johnson KA, Peterson FC, Frederick RO, Zhao Q, Thao S, et al. (October 2004). "Crystal structure of the protein from gene At3g17210 of Arabidopsis thaliana". Proteins. 57 (1): 218–220. doi:10.1002/prot.20215. PMID 15326607.
  2. ↑ Liu Q, Pinto D, Mascher T (November 2018). "Characterization of the Widely Distributed Novel ECF42 Group of Extracytoplasmic Function σ Factors in Streptomyces venezuelae". Journal of Bacteriology. 200 (21): e00437–18. doi:10.1128/JB.00437-18. PMC 6182237. PMID 30126941.
  3. 1 2 "InterPro". www.ebi.ac.uk. Retrieved 2025-03-28.
  4. ↑ "InterPro". www.ebi.ac.uk. Retrieved 2025-04-04.
  5. ↑ "InterPro". www.ebi.ac.uk. Retrieved 2025-03-28.
  6. ↑ Sciara G, Kendrew SG, Miele AE, Marsh NG, Federici L, Malatesta F, et al. (January 2003). "The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis". The EMBO Journal. 22 (2): 205–215. doi:10.1093/emboj/cdg031. hdl:2027.42/102255. PMC 140106. PMID 12514126.
  7. ↑ Katti SK, Katz BA, Wyckoff HW (February 1989). "Crystal structure of muconolactone isomerase at 3.3 A resolution". Journal of Molecular Biology. 205 (3): 557–571. doi:10.1016/0022-2836(89)90226-x. PMID 2926818.
  8. ↑ Leonard PM, Smits SH, Sedelnikova SE, Brinkman AB, de Vos WM, van der Oost J, et al. (March 2001). "Crystal structure of the Lrp-like transcriptional regulator from the archaeon Pyrococcus furiosus". The EMBO Journal. 20 (5): 990–997. doi:10.1093/emboj/20.5.990. PMC 145483. PMID 11230123.