Crystal structure of the plant epigenetic protein arginine methyltransferase 10.
Crystal structure of the plant epigenetic protein arginine methyltransferase 10.
复制标题
植物表观遗传蛋白精氨酸转移酶10的晶体结构10。
DOI:
10.1016/j.jmb.2011.09.040
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发表时间:
2011-11-18
影响因子:
5.6
通讯作者:
Redinbo, Matthew R.
中科院分区:
文献类型:
--
作者:
Cheng, Yuan;Frazier, Monica;Lu, Falong;Cao, Xiaofeng;Redinbo, Matthew R.
Protein arginine methyltransferase 10 (PRMT10) is a type-I arginine methyltransferase essential for regulating flowering time in Arabidopsis thaliana (At). We present a 2.6 Å resolution crystal structure of AtPRMT10 in complex with a reaction product, S-adenosylhomocysteine. The structure reveals a dimerization arm 12–20 residues longer than PRMT structures elucidated previously; as a result, the essential AtPRMT10 dimer exhibits a large central cavity and a distinctly accessible active site. We employ molecular dynamics to examine how dimerization facilitates AtPRMT10 motions necessary for activity, and show that these motions are conserved in other PRMT enzymes. Finally, functional data reveal that the N-terminal ten residues of AtPRMT10 influence substrate specificity, and that enzyme activity is dependent on substrate protein sequences distal from the methylation site. Taken together, these data provide insights into the molecular mechanism of Arabidopsis thaliana PRMT10 as well as other members of the PRMT family of enzymes. They highlight differences between AtPRMT10 and other PRMTs, but also indicate that motions are a conserved element of PRMT function.
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影响因子:
4
作者:
Bedford, Mark T.
通讯作者:
Bedford, Mark T.
影响因子:
4.8
作者:
Goulet, Isabelle;Gauvin, Gabrielle;Cote, Jocelyn
通讯作者:
Cote, Jocelyn
DOI:
10.1016/s1387-2656(08)00008-2
发表时间:
2008-01-01
期刊:
BIOTECHNOLOGY ANNUAL REVIEW, VOL 14
影响因子:
--
作者:
Aletta, John M.;Hu, John C.
通讯作者:
Hu, John C.
影响因子:
7.7
作者:
Niu, Lifang;Lu, Falong;Cao, Xiaofeng
通讯作者:
Cao, Xiaofeng
影响因子:
3
作者:
Duan, Y;Wu, C;Kollman, P
通讯作者:
Kollman, P