2L54
Solution structure of the Zalpha domain mutant of ADAR1 (N43A,Y47A)
Summary for 2L54
| Entry DOI | 10.2210/pdb2l54/pdb |
| Descriptor | Double-stranded RNA-specific adenosine deaminase (1 entity in total) |
| Functional Keywords | hydrolase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: P55265 |
| Total number of polymer chains | 1 |
| Total formula weight | 6943.07 |
| Authors | Zhao, J.,Pervushin, K.,Feng, S.,Droge, P. (deposition date: 2010-10-24, release date: 2011-01-12, Last modification date: 2024-05-01) |
| Primary citation | Feng, S.,Li, H.,Zhao, J.,Pervushin, K.,Lowenhaupt, K.,Schwartz, T.U.,Droge, P. Alternate rRNA secondary structures as regulators of translation Nat.Struct.Mol.Biol., 18:169-176, 2011 Cited by PubMed Abstract: Structural dynamics of large molecular assemblies are intricately linked to function. For ribosomes, macromolecular changes occur especially during mRNA translation and involve participation of ribosomal RNA. Without suitable probes specific to RNA secondary structure, however, elucidation of more subtle dynamic ribosome structure-function relationships, especially in vivo, remains challenging. Here we report that the Z-DNA- and Z-RNA-binding domain Zα, derived from the human RNA editing enzyme ADAR1-L, binds with high stability to specific rRNA segments of Escherichia coli and human ribosomes. Zα impaired in Z-RNA recognition does not associate with ribosomes. Notably, Zα(ADAR1)-ribosome interaction blocks translation in vitro and in vivo, with substantial physiological consequences. Our study shows that ribosomes can be targeted by a protein that specifically recognizes an alternate rRNA secondary structure, and suggests a new mechanism of translational regulation on the ribosome. PubMed: 21217697DOI: 10.1038/nsmb.1962 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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