Adenosine dimethyltransferase: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
The active site pocket of KsgA contains residues N113 and L114 which are part of motif IV SAM-dependent methyltrasferase sequence.  The active site can acomodate both adenosine and methyladenosine.
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Revision as of 10:24, 28 October 2015


Function

Adenosine dimethyltransferase (KsgA) dimethylates two adjacent adenines at the C-terminal of the 16S rRNA in the small 30S ribosomal subunit, thus modifying it. KsgA catalyzes the dimethylation of adenines 1518-1519 using S-adenosyl-methionine (SAM) as the methyl donor and producing S-adenosyl-homocysteine (SAH).

Disease

Relevance

KsgA confers resistance to the antibiotic kasugomycin.

Structural highlights

The active site pocket of KsgA contains residues N113 and L114 which are part of motif IV SAM-dependent methyltrasferase sequence. The active site can acomodate both adenosine and methyladenosine.

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

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3D structures of adenosine dimethyltransferase3D structures of adenosine dimethyltransferase

Updated on 28-October-2015


ReferencesReferences

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky