Structural highlights
Function
[ALKB5_DANRE] Dioxygenase that demethylates RNA by oxidative demethylation: specifically demethylates N(6)-methyladenosine (m(6)A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes. Requires molecular oxygen, alpha-ketoglutarate and iron (By similarity).
Publication Abstract from PubMed
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 1.65A. 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.
Crystal structure of the RNA demethylase ALKBH5 from zebrafish.,Chen W, Zhang L, Zheng G, Fu Y, Ji Q, Liu F, Chen H, He C FEBS Lett. 2014 Mar 18;588(6):892-8. doi: 10.1016/j.febslet.2014.02.021. Epub, 2014 Feb 20. PMID:24561204[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chen W, Zhang L, Zheng G, Fu Y, Ji Q, Liu F, Chen H, He C. Crystal structure of the RNA demethylase ALKBH5 from zebrafish. FEBS Lett. 2014 Mar 18;588(6):892-8. doi: 10.1016/j.febslet.2014.02.021. Epub, 2014 Feb 20. PMID:24561204 doi:http://dx.doi.org/10.1016/j.febslet.2014.02.021
