User:Anika Zohra Yasin/Sandbox1 3pb3
From Proteopedia
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Introduction
NpmA is a methyltransferase or a type of enzyme that methylates one nucleotide in bacterial ribosomes, that contains the structures 3p2e, 3p2i, 3p2k, 3pb3, and 3mte. 3pb3 specifically methylates on the 16S rRNA at the N1 position of A1408. This enzyme belongs to the Kanamycin apramycin methyltransferase (Kam) family. They help create resistance to aminoglycosides, which function as effective antibiotics against certain types of bacteria.
Bactericidal antibiotics are commonly used to treat diseases caused by gram-negative and gram-positive bacteria. Due to the indiscriminate and increased use, bacteria have evolved and formed resistance to these aminoglycoside antibiotics. The different forms of resistance created to these antibiotics include inactivation by alteration, mutation of the small ribosomal subunit to modify the target site of the antibiotic, or methylation at specific sites on the 16S rRNA to prevent the binding of the antibiotic to the ribosome.
The antibiotic binds in a tight pocket on the small subunit of the ribosome, disrupting the pairing of codons and anti-codons. A clinical isolate of E.Coli has been found to possess, 3pb3, an enzyme that adds methyl groups and modifies specific bases in their ribosome, making this pocket unable to fit the antibiotic.
Biological Source
- E. Coli
Structure
Sequence
- Ligand Information: S-ADENOSYL-L-HOMOCYSTEINE(SAH)
Function
- Methyltransferase Activity
3pb3 acts as a methyltransferase also known as methylase which adds a methyl group to specific bases in their ribosomes.
- Antibiotic Resistance
The antibiotic is unable to bind to the ribosomes rendering it ineffective.
