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7OZQ

Crystal structure of archaeal L7Ae bound to eukaryotic kink-loop

Summary for 7OZQ
Entry DOI10.2210/pdb7ozq/pdb
Descriptor50S ribosomal protein L7Ae, RNA, ACETATE ION, ... (7 entities in total)
Functional Keywordsribosomal protein, ribosome
Biological sourcePyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
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Total number of polymer chains8
Total formula weight97301.44
Authors
Hoefler, S.,Lukat, P.,Carlomagno, T.,Blankenfeldt, W. (deposition date: 2021-06-28, release date: 2021-10-27, Last modification date: 2024-01-31)
Primary citationHofler, S.,Lukat, P.,Blankenfeldt, W.,Carlomagno, T.
Eukaryotic Box C/D methylation machinery has two non-symmetric protein assembly sites.
Sci Rep, 11:17561-17561, 2021
Cited by
PubMed Abstract: Box C/D ribonucleoprotein complexes are RNA-guided methyltransferases that methylate the ribose 2'-OH of RNA. The central 'guide RNA' has box C and D motifs at its ends, which are crucial for activity. Archaeal guide RNAs have a second box C'/D' motif pair that is also essential for function. This second motif is poorly conserved in eukaryotes and its function is uncertain. Conflicting literature data report that eukaryotic box C'/D' motifs do or do not bind proteins specialized to recognize box C/D-motifs and are or are not important for function. Despite this uncertainty, the architecture of eukaryotic 2'-O-methylation enzymes is thought to be similar to that of their archaeal counterpart. Here, we use biochemistry, X-ray crystallography and mutant analysis to demonstrate the absence of functional box C'/D' motifs in more than 80% of yeast guide RNAs. We conclude that eukaryotic Box C/D RNPs have two non-symmetric protein assembly sites and that their three-dimensional architecture differs from that of archaeal 2'-O-methylation enzymes.
PubMed: 34475498
DOI: 10.1038/s41598-021-97030-y
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.91 Å)
Structure validation

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