Structural highlights
Function
Q81BA8_BACCR
Publication Abstract from PubMed
The recently discovered HEAT-like repeat (HLR) DNA glycosylase superfamily is widely distributed in all domains of life. The present bioinformatics and phylogenetic analysis shows that HLR DNA glycosylase superfamily members in the genus Bacillus form three subfamilies: AlkC, AlkD and AlkF/AlkG. The crystal structure of AlkF shows structural similarity with the DNA glycosylases AlkC and AlkD, however neither AlkF nor AlkG display any DNA glycosylase activity. Instead, both proteins have affinity to branched DNA structures such as three-way and Holliday junctions. A unique beta-hairpin in the AlkF/AlkG subfamily is most likely inserted into the DNA major groove, and could be a structural determinant regulating DNA substrate affinity. We conclude that AlkF and AlkG represent a new family of HLR proteins with affinity for branched DNA structures.
A new family of proteins related to the HEAT-like repeat DNA glycosylases with affinity for branched DNA structures.,Backe PH, Simm R, Laerdahl JK, Dalhus B, Fagerlund A, Okstad OA, Rognes T, Alseth I, Kolsto AB, Bjoras M J Struct Biol. 2013 Apr 25. pii: S1047-8477(13)00107-X. doi:, 10.1016/j.jsb.2013.04.007. PMID:23623903[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Backe PH, Simm R, Laerdahl JK, Dalhus B, Fagerlund A, Okstad OA, Rognes T, Alseth I, Kolsto AB, Bjoras M. A new family of proteins related to the HEAT-like repeat DNA glycosylases with affinity for branched DNA structures. J Struct Biol. 2013 Apr 25. pii: S1047-8477(13)00107-X. doi:, 10.1016/j.jsb.2013.04.007. PMID:23623903 doi:10.1016/j.jsb.2013.04.007
