Adenosine dimethyltransferase

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== Structural highlights ==
== Structural highlights ==
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Among methyltransferases, KsgA and the reaction it catalyzes are conserved throughout evolution. However, the specifics of substrate recognition by the enzyme remain unknown. Here we report structures of <scene name='59/597431/Cv/2'>Aquifex aeolicus KsgA, in its ligand-free form, in complex with RNA, and in complex with both RNA and S-adenosylhomocysteine</scene> (SAH, reaction product of cofactor S-adenosylmethionine), revealing critical structural information on KsgA-RNA and KsgA-SAH interactions. Moreover, the structures show how conformational changes that occur upon RNA binding create the cofactor-binding site. There are nine conserved functional motifs (motifs I-VIII and X) in KsgA. Prior to RNA binding, motifs I and VIII are flexible, each exhibiting two distinct conformations. Upon RNA binding, the two motifs become stabilized in one of these conformations, which is compatible with the binding of SAH. Motif X, which is also stabilized upon RNA binding, is directly involved in the binding of SAH.<ref>PMID:19278652</ref>
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Among methyltransferases, KsgA and the reaction it catalyzes are conserved throughout evolution. However, the specifics of substrate recognition by the enzyme remain unknown. Here we report structures of <scene name='59/597431/Cv/3'>Aquifex aeolicus KsgA, in its ligand-free form, in complex with RNA, and in complex with both RNA and S-adenosylhomocysteine</scene> (SAH, reaction product of cofactor S-adenosylmethionine), revealing critical structural information on KsgA-RNA and KsgA-SAH interactions. Moreover, the structures show how conformational changes that occur upon RNA binding create the cofactor-binding site. There are nine conserved functional motifs (motifs I-VIII and X) in KsgA. Prior to RNA binding, motifs I and VIII are flexible, each exhibiting two distinct conformations. Upon RNA binding, the two motifs become stabilized in one of these conformations, which is compatible with the binding of SAH. Motif X, which is also stabilized upon RNA binding, is directly involved in the binding of SAH.<ref>PMID:19278652</ref>
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Revision as of 10:59, 20 December 2018

Structure of adenosine dimethyltransferase complex with RNA, SAH and K+ ion (purple) (PDB code 3ftf).

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3D structures of adenosine dimethyltransferase

Updated on 20-December-2018


References

  1. ↑ Tu C, Tropea JE, Austin BP, Court DL, Waugh DS, Ji X. Structural basis for binding of RNA and cofactor by a KsgA methyltransferase. Structure. 2009 Mar 11;17(3):374-85. PMID:19278652 doi:10.1016/j.str.2009.01.010

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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