RsmH catalyses the N4-methylation of cytosine1402 and RsmI (EC 220.127.116.11) catalyses the 2'-O-methylation of cytosine1402 in 16S rRNA. Both methylations are necessary for efficient translation initiation at the UUG and GUG codons.
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
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
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purified recombinant His6-tagged RsmH in complex with S-adenosyl-L-methionine and cytidine in a 1:5:5 ratio, sitting drop vapour diffusion method, from 20 mM Tris, 100 mM NaCl, 5% v/v glycerol, 2 mM DTT, pH 8.0, room temperature, the best crystal is obtained in the mixture solution 1.0 M ammonium sulfate, 0.1 M HEPES, pH 6.5, and 0.5% w/v PEG 8, 000 in 3-4 days, X-ray diffraction structure determination and analysis at 2.25 A resolution