Literature summary for 2.1.1.180 extracted from

Vinal, K.; Conn, G.
Substrate recognition and modification by a pathogen-associated aminoglycoside resistance 16S rRNA methyltransferase (2017), Antimicrob. Agents Chemother., 61, e00077 .

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Application

Application	Comment	Organism
analysis	development of a fluorescence-based binding assay for 30S-NpmA interaction	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Escherichia coli

Crystallization (Comment)

Organism

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

Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
E184C	introduction of a residue displaying high modification efficiency with other Cys-reactive reagents for fluorescence assays. Mutant binds to 30S and dissociates upon addition of SAM	Escherichia coli
E188C	introduction of a residue displaying high modification efficiency with other Cys-reactive reagents for fluorescence assays. Mutant binds to 30S but fails to dissociate upon addition of SAM	Escherichia coli
K131C	introduction of a residue displaying high modification efficiency with other Cys-reactive reagents for fluorescence assays. Mutation blocks 30S-NpmA interaction	Escherichia coli
S89C	introduction of a residue displaying high modification efficiency with other Cys-reactive reagents for fluorescence assays. Mutant binds to 30S but fails to dissociate upon addition of SAM	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	A8C927	-	-