2.1.1.199: 16S rRNA (cytosine1402-N4)-methyltransferase
This is an abbreviated version!
For detailed information about 16S rRNA (cytosine1402-N4)-methyltransferase, go to the full flat file.
Reaction
Synonyms
methyltransferase RsmH, mraW, RsmH
ECTree
Advanced search results
General Information
General Information on EC 2.1.1.199 - 16S rRNA (cytosine1402-N4)-methyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
malfunction
physiological function
both the 2'-O-methylation (catalyzed by RsmI) and N4-methylation of C1402 (catalyzed by RsmH) are needed for efficient initiation at the UUG and GUG codon. m4Cm1402 in the 16S rRNA modulates the accuracy of P-site function. The modification is needed for efficient translation initiation at the UUG and GUG codons
additional information
strain DELTAmraW produces monomethylated cytosine1402 instead of dimethylated C1402 produced by the wild-type enzyme
malfunction
-
enzyme deletion affects efficiency of non-AUG initiation and the fidelity of translation
malfunction
-
enzyme deletion affects efficiency of non-AUG initiation and the fidelity of translation
-
malfunction
-
enzyme deletion affects efficiency of non-AUG initiation and the fidelity of translation
-
RsmH in complex with S-adenosyl-L-methionine and cytidine consists of two distinct but structurally related domains: the typical MTase domain and the putative substrate recognition and binding domain. A deep pocket occurs in the conserved AdoMet binding domain, cytidine binds far from S-adenosyl-L-methionine with the distance of 25.9 A, The complex is not in a catalytically active state, and structural rearrangement of RsmH or the nucleotides neighboring C1402 may be necessary to trigger catalysis
additional information
-
RsmH in complex with S-adenosyl-L-methionine and cytidine consists of two distinct but structurally related domains: the typical MTase domain and the putative substrate recognition and binding domain. A deep pocket occurs in the conserved AdoMet binding domain, cytidine binds far from S-adenosyl-L-methionine with the distance of 25.9 A, The complex is not in a catalytically active state, and structural rearrangement of RsmH or the nucleotides neighboring C1402 may be necessary to trigger catalysis