IPR004498
Ribosomal protein L11 methyltransferase
InterPro entry
Short name | Ribosomal_PrmA_MeTrfase |
Overlapping homologous superfamilies |
Description
Ribosomal protein L11 methyltransferase (PrmA) (
2.1.1) is required for the methylation of ribosomal protein L11. It forms a bifunctional operon in Escherichia coli with panF (pantothenate transport). In E. coli, it trimethylates the N-terminal alpha-amino group and the ε-amino groups of Lys3 and Lys39
[1]. In Arabidopsis is targeted to both mitochondria and chloroplasts. Structures comparison with the E. coli enzyme revealed that they share similar product specificity but display a difference in substrate site specificity
[2].
References
1.Multiple-site trimethylation of ribosomal protein L11 by the PrmA methyltransferase. Demirci H, Gregory ST, Dahlberg AE, Jogl G. Structure 16, 1059-66, (2008). View articlePMID: 18611379
2.Dual Targeting of the Protein Methyltransferase PrmA Contributes to Both Chloroplastic and Mitochondrial Ribosomal Protein L11 Methylation in Arabidopsis. Mazzoleni M, Figuet S, Martin-Laffon J, Mininno M, Gilgen A, Leroux M, Brugiere S, Tardif M, Alban C, Ravanel S. Plant Cell Physiol 56, 1697-710, (2015). PMID: 26116422
GO terms
biological process
molecular function
cellular component
- None
Cross References
ENZYME
Contributing Member Database Entries
- PIRSF:PIRSF000401
- HAMAP:MF_00735
- NCBIfam:TIGR00406
Representative structure
2nxc: Apo-form of T. thermophilus ribosomal protein L11 methyltransferase (PrmA)