Multiple-site trimethylation of ribosomal protein L11 by the PrmA methyltransferase.
Multiple-site trimethylation of ribosomal protein L11 by the PrmA methyltransferase.
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DOI：
10.1016/j.str.2008.03.016
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发表时间：
2008-07
期刊：
影响因子：
--
通讯作者：
Jogl G
中科院分区：
文献类型：
--
作者：
Demirci H;Gregory ST;Dahlberg AE;Jogl G
Ribosomal protein L11 is a universally conserved component of the large subunit, and plays a significant role during initiation, elongation, and termination of protein synthesis. In Escherichia coli, the lysine methyltransferase PrmA trimethylates the N-terminal α-amino group and the ε-amino groups of Lys3 and Lys39. Here, we report four PrmA-L11 complex structures in different orientations with respect to the PrmA active site. Two structures capture the L11 N-terminal α-amino group in the active site in a trimethylated postcatalytic state and in a dimethylated state with bound S-adenosyl-L-homocysteine. Two other structures show L11 in a catalytic orientation to modify Lys39 and in a noncatalytic orientation. The comparison of complex structures in different orientations with a minimal substrate recognition complex shows that the binding mode remains conserved in all L11 orientations, and that substrate orientation is brought about by the unusual interdomain flexibility of PrmA.
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影响因子：
3.2
作者：
Cameron, DM;Gregory, ST;Dahlberg, AE
通讯作者：
Dahlberg, AE
DOI：
10.1111/j.1432-1033.1980.tb04995.x
发表时间：
1980-01-01
期刊：
EUROPEAN JOURNAL OF BIOCHEMISTRY
影响因子：
--
作者：
DOGNIN, MJ;WITTMANNLIEBOLD, B
通讯作者：
WITTMANNLIEBOLD, B
影响因子：
4.8
作者：
Patnaik, D;Chin, HG;Pradhan, S
通讯作者：
Pradhan, S
DOI：
10.1038/nsb946
发表时间：
2003-07-01
期刊：
NATURE STRUCTURAL BIOLOGY
影响因子：
--
作者：
Trievel, RC;Flynn, EM;Hurley, JH
通讯作者：
Hurley, JH
DOI：
10.1107/s0907444904019158
发表时间：
2004-12-01
影响因子：
2.2
作者：
Emsley, P;Cowtan, K
通讯作者：
Cowtan, K