Biology:Dim A B barrel

From HandWiki
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
InterProIPR011008

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, Craig A; Johnson, Kenneth A; Peterson, Francis C; Frederick, Ronnie O; Zhao, Qin; Thao, Sandy; Fox, Brian G; Volkman, Brian F et al. (2004-10-01). "Crystal structure of the protein from gene At3g17210 of Arabidopsis thaliana". Proteins 57 (1): 218–220. doi:10.1002/prot.20215. ISSN 1097-0134. PMID 15326607. https://europepmc.org/article/MED/15326607. 
  2. ↑ Liu, Qiang; Pinto, Daniela; Mascher, Thorsten (2018-11-01). "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. ISSN 1098-5530. PMID 30126941. 
  3. ↑ 3.0 3.1 "InterPro". https://www.ebi.ac.uk/interpro/set/pfam/CL0032/. 
  4. ↑ "InterPro". https://www.ebi.ac.uk/interpro/entry/InterPro/IPR011008/. 
  5. ↑ "InterPro". https://www.ebi.ac.uk/interpro/entry/InterPro/IPR011008/. 
  6. ↑ Sciara, Giuliano; Kendrew, Steven G; Miele, Adriana E; Marsh, Neil G; Federici, Luca; Malatesta, Francesco; Schimperna, Giuliana; Savino, Carmelinda et al. (2003-01-01). "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. ISSN 1460-2075. PMID 12514126. 
  7. ↑ Katti, S K; Katz, B A; Wyckoff, H W (1989-02-01). "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. ISSN 1089-8638. PMID 2926818. 
  8. ↑ Leonard, P M; Smits, S H; Sedelnikova, S E; Brinkman, A B; de Vos, W M; van der Oost, J; Rice, D W; Rafferty, J B (2001-03-01). "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. ISSN 1460-2075. PMID 11230123. 



Retrieved from "https://handwiki.org/wiki/index.php?title=Biology:Dim_A_B_barrel&oldid=4103317"