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Literature summary for 2.1.1.193 extracted from

  • Zhang, H.; Wan, H.; Gao, Z.Q.; Wei, Y.; Wang, W.J.; Liu, G.F.; Shtykova, E.V.; Xu, J.H.; Dong, Y.H.
    Insights into the catalytic mechanism of 16S rRNA methyltransferase RsmE (m3U1498) from crystal and solution structures (2012), J. Mol. Biol., 423, 576-589.
    View publication on PubMed
Search for more literature for 2.1.1.193

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop vapor diffusion method at room temperature, 0.15 M potassium thiocyanate and 24% w/v PEG monomethyl ether 2000, 3-4 days, crystal soaking in S-adenosyl-L-methionine solution or cocrystallization of enzyme and cofactor are not successful, X-ray diffraction structure determination and analysis at 2.25 A resolution, molecular replacement Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information thermodynamics of S-adenosyl-L-methionine binding by RsmE, thermodynamic analysis, overview Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + uracil1498 in 16S rRNA Escherichia coli RsmE requires a highly structured ribonucleoprotein particle (a fully assembled 30S ribosome subunit) as a substrate for methylation, and this methylation occurs late during 30S ribosome assembly S-adenosyl-L-homocysteine + N3-methyluracil1498 in 16S rRNA
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AGL7 gene rsmE
-

Reaction

Reaction Comment Organism Reaction ID
S-adenosyl-L-methionine + uracil1498 in 16S rRNA = S-adenosyl-L-homocysteine + N3-methyluracil1498 in 16S rRNA structure-function relationship and catalytic mechanism, overview Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + uracil1498 in 16S rRNA
-
 Escherichia coli S-adenosyl-L-homocysteine + N3-methyluracil1498 in 16S rRNA
-
 ?
S-adenosyl-L-methionine + uracil1498 in 16S rRNA RsmE requires a highly structured ribonucleoprotein particle (a fully assembled 30S ribosome subunit) as a substrate for methylation, and this methylation occurs late during 30S ribosome assembly Escherichia coli S-adenosyl-L-homocysteine + N3-methyluracil1498 in 16S rRNA
-
 ?

Subunits

Subunits Comment Organism
homodimer the crystal structure in monomer shows that RsmE consists of two distinct but structurally related domains: the pseudouridine synthases and archaeosine-specific transglycosylasess-like RNA recognition and binding domain, PUA, and the conserved MTase domain with a deep trefoil knot Escherichia coli
More the methylation process is required by collaboration of both subunits, and dimerization is functionally critical for catalysis. Molecular replacement of crystal structure, PDB ID 1VHY. Structural comparisons of N-terminal and C-terminal domains of RsmE with related proteins, overview Escherichia coli

Synonyms

Synonyms Comment Organism
16S rRNA methyltransferase
-
 Escherichia coli
RsmE
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine one molecule bound per subunit of the enzyme homodimer Escherichia coli

General Information

General Information Comment Organism
evolution RsmE is the founding member of a RNA methyltransferase family responsible for N3-methylation of U1498 in 16S ribosomal RNA. It is well conserved across bacteria and plants and may play an 30 important role in ribosomal intersubunit communication Escherichia coli
additional information RsmE forms a flexible dimeric conformation that is essential for substrate binding. RsmE-S-adenosyl-L-methionine-uridylic acid complex modeling and substrate binding structure, overview. The MTase domain of one subunit in dimeric RsmE is responsible for binding of one S-adenosyl-L-methionine molecule and catalytic process while the PUA-like domain in the other subunit is mainly responsible for recognition of one substrate molecule, the ribosomal RNA fragment and ribosomal protein complex. The methylation process is required by collaboration of both subunits, and dimerization is functionally critical for catalysis. Molecular replacement of crystal structure, PDB ID 1VHY Escherichia coli
physiological function RsmE is responsible for methylation of U1498 in 16S ribosomal RNA in Escherichia coli Escherichia coli