5XJ1

Crystal structure of spRlmCD

Summary for 5XJ1

• Entry DOI: 10.2210/pdb5xj1/pdb
• Related: 5XJ2
• Descriptor: Uncharacterized RNA methyltransferase SP_1029, GLYCEROL, HEXAETHYLENE GLYCOL, ... (5 entities in total)
• Functional Keywords: 23s rrna, u747, methyltransferase, transferase
• Biological source: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
• Total number of polymer chains: 1
• Total formula weight: 52091.86

Authors

Jiang, Y.,Gong, Q. (deposition date: 2017-04-28, release date: 2017-11-01, Last modification date: 2023-11-22)

Primary citation

Jiang, Y.,Li, F.,Wu, J.,Shi, Y.,Gong, Q.
Structural insights into substrate selectivity of ribosomal RNA methyltransferase RlmCD
PLoS ONE, 12:e0185226-e0185226, 2017

PubMed Abstract: RlmCD has recently been identified as the S-adenosyl methionine (SAM)-dependent methyltransferase responsible for the formation of m5U at U747 and U1939 of 23S ribosomal RNA in Streptococcus pneumoniae. In this research, we determine the high-resolution crystal structures of apo-form RlmCD and its complex with SAH. Using an in-vitro methyltransferase assay, we reveal the crucial residues for its catalytic functions. Furthermore, structural comparison between RlmCD and its structural homologue RumA, which only catalyzes the m5U1939 in Escherichia coli, implicates that a unique long linker in the central domain of RlmCD is the key factor in determining its substrate selectivity. Its significance in the enzyme activity of RlmCD is further confirmed by in-vitro methyltransferase assay.

PubMed: 28949991
DOI: 10.1371/journal.pone.0185226

Experimental method

X-RAY DIFFRACTION (1.753 Å)