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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Cubrilo, Sonja Bujnicki, Janusz M. Tkaczuk, Karolina L. Maravic Vlahovicek, Gordana |
| Description | Author Affiliation: Maravic Vlahovicek G ( Department of Biochemistry and Molecular Biology, Faculty of Pharmacy and Biochemistry, University of Zagreb, Ante Kovacica 1, 10000 Zagreb, Croatia. gordana@pharma.hr) |
| Abstract | Methyltransferases that carry out posttranscriptional N $^{7}$ -methylation of G1405 in 16S rRNA confer bacterial resistance to aminoglycoside antibiotics, including kanamycin and gentamicin. Genes encoding enzymes from this family (hereafter referred to as Arm, for aminoglycoside resistance methyltransferases) have been recently found to spread by horizontal gene transfer between various human pathogens. The knowledge of the Arm protein structure would lay the groundwork for the development of potential resistance inhibitors, which could be used to restore the potential of aminoglycosides to act against the resistant pathogens. We analyzed the sequence–function relationships of Sgm MTase, a member of the Arm family, by limited proteolysis and site-directed and random mutagenesis. We also modeled the structure of Sgm using bioinformatics techniques and used the model to provide a structural context for experimental results. We found that Sgm comprises two domains and we characterized a number of functionally compromised point mutants with substitutions of invariant or conserved residues. Our study provides a low-resolution (residue-level) model of sequence–structure–function relationships in the Arm family of enzymes and reveals the cofactor-binding and substrate-binding sites. These functional regions will be prime targets for further experimental and theoretical studies aimed at defining the reaction mechanism of m $^{7}$ G1405 methylation, increasing the resolution of the model and developing Arm-specific inhibitors. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 4 |
| Volume Number | 1784 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2008-04-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Aminoglycosides Pharmacology Drug Resistance, Bacterial Methyltransferases Chemistry Amino Acid Sequence Anti-Bacterial Agents Bacterial Proteins Genetics Computational Biology Gentamicins Kanamycin Micromonospora Classification Drug Effects Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Phylogeny Protein Structure, Secondary Protein Structure, Tertiary Sequence Homology, Amino Acid Structure-Activity Relationship Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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