| Structural highlights
Function
[DODEC_HALS3] May function as storage protein that sequesters riboflavin and related compounds, thereby protecting the cell against undesirable reactions mediated by the free flavins. Binds and sequesters riboflavin, lumiflavin and lumichrome. Can also bind FAD and FMN (in vitro), but has low affinity for FAD and even lower affinity for FMN. Protects bound flavins against light damage; Trp-36 rapidly quenches the flavin excited state. Promotes the conversion of bound riboflavin to lumichrome.[1] [2] [3] [4] [5]
References
- ↑ Bieger B, Essen LO, Oesterhelt D. Crystal structure of halophilic dodecin: a novel, dodecameric flavin binding protein from Halobacterium salinarum. Structure. 2003 Apr;11(4):375-85. PMID:12679016
- ↑ Grininger M, Zeth K, Oesterhelt D. Dodecins: a family of lumichrome binding proteins. J Mol Biol. 2006 Mar 31;357(3):842-57. Epub 2006 Jan 18. PMID:16460756 doi:10.1016/j.jmb.2005.12.072
- ↑ Grininger M, Seiler F, Zeth K, Oesterhelt D. Dodecin sequesters FAD in closed conformation from the aqueous solution. J Mol Biol. 2006 Dec 8;364(4):561-6. Epub 2006 Sep 5. PMID:17027852 doi:10.1016/j.jmb.2006.08.083
- ↑ Grininger M, Staudt H, Johansson P, Wachtveitl J, Oesterhelt D. Dodecin is the key player in flavin homeostasis of archaea. J Biol Chem. 2009 May 8;284(19):13068-76. Epub 2009 Feb 17. PMID:19224924 doi:10.1074/jbc.M808063200
- ↑ Grininger M, Noll G, Trawoger S, Sinner EK, Oesterhelt D. Electrochemical switching of the flavoprotein dodecin at gold surfaces modified by flavin-DNA hybrid linkers. Biointerphases. 2008 Sep;3(3):51-8. PMID:20408700 doi:10.1116/1.2965134
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