期刊
STRUCTURE
卷 16, 期 7, 页码 1059-1066出版社
CELL PRESS
DOI: 10.1016/j.str.2008.03.016
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资金
- NIBIB NIH HHS [P30 EB009998] Funding Source: Medline
- NIGMS NIH HHS [R01 GM019756, R01 GM019756-36, F32 GM019756, GM19756] Funding Source: Medline
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 alpha-amino group and the epsilon-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 alpha-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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