ArticleThe Journal of biological chemistry2010
Structure of the antibiotic resistance factor spectinomycin phosphotransferase from Legionella pneumophila.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 40 citations in OpenAlex.
- Comparison of Phenotypic and Whole-Genome Sequencing-Derived Antimicrobial Resistance Profiles ofAntibiotics (Basel, Switzerland) · 2025Article
- Comparative genome analysis investigation of nosocomial and community-acquired cases of Legionnaires' disease caused by ST2858 and ST378.Microbiology spectrum · 2025Article
- Identification and characterization of a novel chromosome-encoded aminoglycosideFrontiers in microbiology · 2024Article
- Pan-kinome of Legionella expanded by a bioinformatics survey.Scientific reports · 2022Article
- Genomic characterization and assessment of pathogenic potential ofFrontiers in microbiology · 2022Article
- Functional characterization of a novel aminoglycoside phosphotransferase, APH(9)-Ic, and its variant fromFrontiers in cellular and infection microbiology · 2022Article
- A kinase bioscavenger provides antibiotic resistance by extremely tight substrate binding.Science advances · 2020Article
- Structural Recognition of Spectinomycin by Resistance Enzyme ANT(9) from Enterococcus faecalis.Antimicrobial agents and chemotherapy · 2020Article
- Structural basis for the substrate recognition of aminoglycoside 7''-phosphotransferase-Ia from Streptomyces hygroscopicus.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Structural and kinetic characterization of (The Journal of biological chemistry · 2018Article
- Structure of the phosphotransferase domain of the bifunctional aminoglycoside-resistance enzyme AAC(6')-Ie-APH(2'')-Ia.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Structure-guided optimization of protein kinase inhibitors reverses aminoglycoside antibiotic resistance.The Biochemical journal · 2013Article
- Strategies to overcome the action of aminoglycoside-modifying enzymes for treating resistant bacterial infections.Future medicinal chemistry · 2013Review
- Prospects for circumventing aminoglycoside kinase mediated antibiotic resistance.Frontiers in cellular and infection microbiology · 2013Review
- Structural basis for dual nucleotide selectivity of aminoglycoside 2''-phosphotransferase IVa provides insight on determinants of nucleotide specificity of aminoglycoside kinases.The Journal of biological chemistry · 2012Article
- Aminoglycoside 2''-phosphotransferase IIIa (APH(2'')-IIIa) prefers GTP over ATP: structural templates for nucleotide recognition in the bacterial aminoglycoside-2'' kinases.The Journal of biological chemistry · 2012Article
- Small-angle X-ray scattering analysis of the bifunctional antibiotic resistance enzyme aminoglycoside (6') acetyltransferase-ie/aminoglycoside (2'') phosphotransferase-ia reveals a rigid solution structure.Antimicrobial agents and chemotherapy · 2012Article
- Crystal structures of two aminoglycoside kinases bound with a eukaryotic protein kinase inhibitor.PloS one · 2011Article
- Structure and function of APH(4)-Ia, a hygromycin B resistance enzyme.The Journal of biological chemistry · 2011Article
- Aminoglycoside modifying enzymes.Drug resistance updates : reviews and commentaries in antimicrobial and anticancer chemotherapy · 2010Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Aminoglycoside phosphotransferases (APHs) constitute a diverse group of enzymes that are often the underlying cause of aminoglycoside resistance in the clinical setting. Several APHs have been extensively characterized, including the elucidation of the three-dimensional structure of two APH(3') isozymes and an APH(2'') enzyme. Although many APHs are plasmid-encoded and are capable of inactivating numerous 2-deoxystreptmaine aminoglycosides with multiple regiospecificity, APH(9)-Ia, isolated from Legionella pneumophila, is an unusual enzyme among the APH family for its chromosomal origin and its specificity for a single non-2-deoxystreptamine aminoglycoside substrate, spectinomycin. We describe here the crystal structures of APH(9)-Ia in its apo form, its binary complex with the nucleotide, AMP, and its ternary complex bound with ADP and spectinomycin. The structures reveal that APH(9)-Ia adopts the bilobal protein kinase-fold, analogous to the APH(3') and APH(2'') enzymes. However, APH(9)-Ia differs significantly from the other two types of APH enzymes in its substrate binding area and that it undergoes a conformation change upon ligand binding. Moreover, kinetic assay experiments indicate that APH(9)-Ia has stringent substrate specificity as it is unable to phosphorylate substrates of choline kinase or methylthioribose kinase despite high structural resemblance. The crystal structures of APH(9)-Ia demonstrate and expand our understanding of the diversity of the APH family, which in turn will facilitate the development of new antibiotics and inhibitors.
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