RsmH catalyses the N4-methylation of cytosine1402 and RsmI (EC 2.1.1.198) catalyses the 2′-O-methylation of cytosine1402 in 16S rRNA. Both methylations are necessary for efficient translation initiation at the UUG and GUG codons.
The enzyme appears in viruses and cellular organisms
RsmH catalyses the N4-methylation of cytosine1402 and RsmI (EC 2.1.1.198) 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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
show
top
