ArticleJournal of molecular biology2009
Structural rearrangements in the active site of the Thermus thermophilus 16S rRNA methyltransferase KsgA in a binary complex with 5'-methylthioadenosine.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
- Structural basis of successive adenosine modifications by the conserved ribosomal methyltransferase KsgA.Nucleic acids research · 2021Article
- Crystal structure of ErmE - 23S rRNA methyltransferase in macrolide resistance.Scientific reports · 2019Article
- Dimethyl adenosine transferase (KsgA) contributes to cell-envelope fitness in Salmonella Enteritidis.Microbiological research · 2018Article
- Recognition Site Generated by Natural Changes in Erm Proteins Leads to Unexpectedly High Susceptibility to Chymotrypsin.ACS omega · 2017Article
- Structural and functional insights into the molecular mechanism of rRNA m6A methyltransferase RlmJ.Nucleic acids research · 2013Article
- Structural basis for S-adenosylmethionine binding and methyltransferase activity by mitochondrial transcription factor B1.Nucleic acids research · 2013Article
- Structural insights into methyltransferase KsgA function in 30S ribosomal subunit biogenesis.The Journal of biological chemistry · 2012Article
- Modification of 16S ribosomal RNA by the KsgA methyltransferase restructures the 30S subunit to optimize ribosome function.RNA (New York, N.Y.) · 2010Article
- Multi-site-specific 16S rRNA methyltransferase RsmF from Thermus thermophilus.RNA (New York, N.Y.) · 2010Article
- The chlamydial functional homolog of KsgA confers kasugamycin sensitivity to Chlamydia trachomatis and impacts bacterial fitness.BMC microbiology · 2009Article
- Structural and functional studies of the Thermus thermophilus 16S rRNA methyltransferase RsmG.RNA (New York, N.Y.) · 2009Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Posttranscriptional modification of ribosomal RNA (rRNA) occurs in all kingdoms of life. The S-adenosyl-L-methionine-dependent methyltransferase KsgA introduces the most highly conserved rRNA modification, the dimethylation of A1518 and A1519 of 16S rRNA. Loss of this dimethylation confers resistance to the antibiotic kasugamycin. Here, we report biochemical studies and high-resolution crystal structures of KsgA from Thermus thermophilus. Methylation of 30S ribosomal subunits by T. thermophilus KsgA is more efficient at low concentrations of magnesium ions, suggesting that partially unfolded RNA is the preferred substrate. The overall structure is similar to that of other methyltransferases but contains an additional alpha-helix in a novel N-terminal extension. Comparison of the apoenzyme with complex structures with 5'-methylthioadenosine or adenosine bound in the cofactor-binding site reveals novel features when compared with related enzymes. Several mobile loop regions that restrict access to the cofactor-binding site are observed. In addition, the orientation of residues in the substrate-binding site indicates that conformational changes are required for binding two adjacent residues of the substrate rRNA.
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