Crystal structure of the RNA demethylase ALKBH5 from zebrafish

详细信息    查看全文

• 作者：Weizhong Chen^a ; ^b ; ^c ; Liang Zhang^b ; Guanqun Zheng^b ; Ye Fu^b ; Quanjiang Ji^b ; Fange Liu^b ; Hao Chen^c ; Chuan He^b ; ^{chuanhe@uchicago.edu" class="auth_mail}
• 关键词：m6A ; N6-methyladenosine ; hm6A ; N6-hydroxymethyladenosine ; fm6A ; N6-formyladenosine ; A ; adenosine ; fALKBH5 ; zebrafish ALKBH5 ; 伪-KG ; 伪-ketoglutarate ; m1A ; 1-methyladenine ; m3C ; 3-methylcytosine ; ss ; single-stranded ; ds ; double-stranded ; cm5U ; 5-carboxy-methyluridine ; (S)-mchm5U ; (S)-5-methoxycarbonyl-hydroxymethyluridine ; m3T ; 3-methylthymine ; m3U ; 3-methyluracil ; 螖fALKBH5 ; truncated zebrafish ALKBH5 ; IPTG ; isopropyl 尾-D-1-thiogalactopyranoside ; SIN ; succinate acid ; hALKBH3 ; human ALKBH3 ; hALK
• 刊名：FEBS Letters
• 出版年：18 March, 2014
• 年：2014
• 卷：588
• 期：6
• 页码：892-898
• 全文大小：1962 K

文摘

ALKBH5, a member of AlkB family proteins, has been reported as a mammalian N⁶-methyladenosine (m⁶A) RNA demethylase. Here we report the crystal structure of zebrafish ALKBH5 (fALKBH5) with the resolution of 1.65 脜. 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 m⁶A RNA demethylases, ALKBH5 and FTO, which may result in their slightly different pathways of m⁶A demethylation.