2.1.1.180: 16S rRNA (adenine1408-N1)-methyltransferase
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For detailed information about 16S rRNA (adenine1408-N1)-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.180
Reaction
Synonyms
16S rRNA (m1A1408) methyltransferase, 16S rRNA m1A1408 methyltransferase, 16S rRNA:m(1)A1408 methyltransferase, A1408 16S rRNA methyltransferase, KAM, KamB, kanamycin-apramycin resistance methylase, Kmr, m1A1408, Npm, NpmA, plasmid-mediated 16S rRNA methyltransferase A, ShKam
ECTree
2.1.1.180 16S rRNA (adenine1408-N1)-methyltransferaseAdvanced search results
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results (Crystallization
Crystallization on EC 2.1.1.180 - 16S rRNA (adenine1408-N1)-methyltransferase
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CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.03 M Bis-Tris (pH 5.5) and 25.5% (w/v) polyethylene glycol 3350
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electrostatic interactions made by the NpmA beta2/3 linker collectively are critical for docking of NpmA on a conserved 16S rRNA tertiary surface. Other NpmA regions (beta5/beta6 and beta6/beta7 linkers) contain several residues critical for optimal positioning of A1408 but are largely dispensable for 30S binding. In a model for NpmA action, 30S binding and adoption of a catalytically competent state are distinct: docking on 16S rRNA via the beta2/3 linker necessarily precedes functionally critical 30S substrate-driven conformational changes elsewhere in NpmA
H/D exchange mass spectrometry of apo NpmA in the presence and absence of SAM/SAH. Ligand binding results in time-dependent differences in deuterium exchange not only at the ligand-binding pocket (residues D25-D55 and A86-E112) but also in distal regions (F62-F82 and Y113-S144) of NpmA
high-resolution crystal structures of NpmA from Escherichia coli is determined at 1.69 A
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apo-enzyme, to 1.8 A resolution, by molecular replacement. Kmr possesses a canonical S-adenosylmethionine binding pocket but with reduced sensitivity to mutation
high-resolution crystal structures of KamB from Streptoalloteichus tenebrarius is determined at 1.69 A
