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. | |||
</StructureSection> | </StructureSection> | ||
Revision as of 10:24, 28 October 2015
FunctionAdenosine 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). DiseaseRelevanceKsgA confers resistance to the antibiotic kasugomycin. Structural highlightsThe 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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3D structures of adenosine dimethyltransferase3D structures of adenosine dimethyltransferase
Updated on 28-October-2015