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8JOZ

Crystal structure of CmoM from E. coli complexed with sinefungin and cellularly expressed tRNA Ser

Summary for 8JOZ
Entry DOI10.2210/pdb8joz/pdb
DescriptortRNA 5-carboxymethoxyuridine methyltransferase, tRNA Ser (88-MER), SINEFUNGIN, ... (5 entities in total)
Functional Keywordsmethyltransferase, trna post-transcriptional modification, cmom mcmo5u, transferase-rna complex, transferase, transferase/rna
Biological sourceEscherichia coli K-12
More
Total number of polymer chains2
Total formula weight61399.68
Authors
Yoo, J.,Kim, J. (deposition date: 2023-06-09, release date: 2023-08-30, Last modification date: 2023-10-04)
Primary citationYoo, J.,Lee, J.,Kim, J.
Structural basis for the selective methylation of 5-carboxymethoxyuridine in tRNA modification.
Nucleic Acids Res., 51:9432-9441, 2023
Cited by
PubMed Abstract: Posttranscriptional modifications of tRNA are widely conserved in all domains of life. Especially, those occurring within the anticodon often modulate translational efficiency. Derivatives of 5-hydroxyuridine are specifically found in bacterial tRNA, where 5-methoxyuridine and 5-carboxymethoxyuridine are the major species in Gram-positive and Gram-negative bacteria, respectively. In certain tRNA species, 5-carboxymethoxyuridine can be further methylated by CmoM to form the methyl ester. In this report, we present the X-ray crystal structure of Escherichia coli CmoM complexed with tRNASer1, which contains 5-carboxymethoxyuridine at the 5'-end of anticodon (the 34th position of tRNA). The 2.22 Å resolution structure of the enzyme-tRNA complex reveals that both the protein and tRNA undergo local conformational changes around the binding interface. Especially, the hypomodified uracil base is flipped out from the canonical stacked conformation enabling the specific molecular interactions with the enzyme. Moreover, the structure illustrates that the enzyme senses exclusively the anticodon arm region of the substrate tRNA and examines the presence of key determinants, 5-carboxymethoxyuridine at position 34 and guanosine at position 35, offering molecular basis for the discriminatory mechanism against non-cognate tRNAs.
PubMed: 37587716
DOI: 10.1093/nar/gkad668
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.22 Å)
Structure validation

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