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Literature summary for 2.1.1.179 extracted from

  • Nosrati, M.; Dey, D.; Mehrani, A.; Strassler, S.E.; Zelinskaya, N.; Hoffer, E.D.; Stagg, S.M.; Dunham, C.M.; Conn, G.L.
    Functionally critical residues in the aminoglycoside resistance-associated methyltransferase RmtC play distinct roles in 30S substrate recognition (2019), J. Biol. Chem., 294, 17642-17653 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with S-adenosylhomocysteine. An N-terminal domain surface within RmtC, comprising basic residues from both the N1 and N2 subdomains, directly contributes to 30S-binding affinity. Additional residues lining a contiguous adjacent surface on the C-terminal domain are critical for 16S rRNA modification but do not directly contribute to the binding affinity Proteus mirabilis

Protein Variants

Protein Variants Comment Organism
H54A inactive. Mutation dos not impact 30S binding affinity. Mutant strain is sensitive to kanamycin and gentamicin Proteus mirabilis
H54E inactive. Mutation dos not impact 30S binding affinity. Mutant strain is sensitive to kanamycin and gentamicin Proteus mirabilis
K20E mutation eliminates 30S binding affinity, mutant strain is sensitive to kanamycin and gentamicin Proteus mirabilis
K72E mutation reduces 30S binding affinity about 5fold, resistance to kanamycin and gentamcin is reduced Proteus mirabilis
additional information replacement of the RmtC loop with four Ala residues (Loop237-246 ->A4) ablates the enzyme's ability to confer resistance to kanamycin and gentamicin. Conserved C-terminal domain residues surrounding the SAM-binding pocket are functionally critical but do not contribute to 30S binding affinity Proteus mirabilis
R50E mutation reduces 30S binding affinity about 11-13fold. Mutant strain is sensitive to kanamycin and gentamicin Proteus mirabilis
R68E mutation reduces 30S binding affinity about 11-13fold, resistance to kanamycin and gentamcin is reduced Proteus mirabilis

Organism

Organism UniProt Comment Textmining
Proteus mirabilis Q33DX5
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Synonyms

Synonyms Comment Organism
RmtC
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Proteus mirabilis