8z62
Crystal structure of rRNA (uracil-C5)-methyltransferase from Pyrococcus horikoshii OT3
Structural highlights
FunctionARLMC_PYRHO Catalyzes the formation of 5-methyl-uridine at position equivalent to 747 (m5U747) in 23S rRNA. Publication Abstract from PubMed5-Methyluridine (m(5)U) rRNA modifications frequently occur at U747 and U1939 (Escherichia coli numbering) in domains II and IV of the 23S rRNA in Gram-negative bacteria, with the help of S-adenosyl-l-methionine (SAM)-dependent rRNA methyltransferases (MTases), RlmC and RlmD, respectively. In contrast, Gram-positive bacteria utilize a single SAM-dependent rRNA MTase, RlmCD, to modify both corresponding sites. Notably, certain archaea, specifically within the Thermococcales group, have been found to possess two genes encoding SAM-dependent archaeal (tRNA and rRNA) m(5)U (Arm(5)U) MTases. Among these, a tRNA-specific Arm(5)U MTase ((Pab)TrmU54) has already been characterized. This study focused on the structural and functional characterization of the rRNA-specific Arm(5)U MTase from the hyperthermophilic archaeon Pyrococcus horikoshii (PhRlmCD). An in-depth structural examination revealed a dynamic hinge movement induced by the replacement of the iron-sulfur cluster with disulfide bonds, obstructing the substrate-binding site. It revealed distinctive characteristics of PhRlmCD, including elongated positively charged loops in the central domain and rotational variations in the TRAM domain, which influence substrate selectivity. Additionally, the results suggested that two potential mini-rRNA fragments interact in a similar manner with PhRlmCD at a positively charged cleft at the interface of domains and facilitate dual MTase activities akin to the protein RlmCD. Altogether, these observations showed that Arm(5)U MTases originated from horizontal gene transfer events, most likely from Gram-positive bacteria. Decoding Substrate Selectivity of an Archaeal RlmCD-like Methyltransferase Through Its Salient Traits.,Saha S, Kanaujia SP Biochemistry. 2024 Oct 1;63(19):2477-2492. doi: 10.1021/acs.biochem.4c00401. Epub , 2024 Sep 18. PMID:39350642[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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