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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Proteus mirabilis | Q33DX5 | - |
- |
Synonyms | Comment | Organism |
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RmtC | - |
Proteus mirabilis |