| Literature DB >> 24561204 |
Weizhong Chen1, Liang Zhang2, Guanqun Zheng2, Ye Fu2, Quanjiang Ji2, Fange Liu2, Hao Chen3, Chuan He4.
Abstract
ALKBH5, a member of AlkB family proteins, has been reported as a mammalian N(6)-methyladenosine (m(6)A) RNA demethylase. Here we report the crystal structure of zebrafish ALKBH5 (fALKBH5) with the resolution of 1.65Å. Structural superimposition shows that fALKBH5 is comprised of a conserved jelly-roll motif. However, it possesses a loop that interferes potential binding of a duplex nucleic acid substrate, suggesting an important role in substrate selection. In addition, several active site residues are different between the two known m(6)A RNA demethylases, ALKBH5 and FTO, which may result in their slightly different pathways of m(6)A demethylation.Entities:
Keywords: ALKBH5; Crystal structure; Demethylation; N(6)-Hydroxymethyladenosine
Mesh:
Substances:
Year: 2014 PMID: 24561204 PMCID: PMC3982313 DOI: 10.1016/j.febslet.2014.02.021
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124