6E4O
Structure of apo T. brucei RRM: P4(1)2(1)2 form
Summary for 6E4O
| Entry DOI | 10.2210/pdb6e4o/pdb |
| Related | 6E4N |
| Descriptor | RNA-binding protein, putative (2 entities in total) |
| Functional Keywords | rrm, rna binding, rna binding protein |
| Biological source | Trypanosoma brucei |
| Total number of polymer chains | 4 |
| Total formula weight | 31194.94 |
| Authors | Schumacher, M.A. (deposition date: 2018-07-18, release date: 2018-12-12, Last modification date: 2023-10-11) |
| Primary citation | Travis, B.,Shaw, P.L.R.,Liu, B.,Ravindra, K.,Iliff, H.,Al-Hashimi, H.M.,Schumacher, M.A. The RRM of the kRNA-editing protein TbRGG2 uses multiple surfaces to bind and remodel RNA. Nucleic Acids Res., 47:2130-2142, 2019 Cited by PubMed Abstract: Kinetoplastid RNA (kRNA) editing takes place in the mitochondria of kinetoplastid protists and creates translatable mRNAs by uridine insertion/deletion. Extensively edited (pan-edited) transcripts contain quadruplex forming guanine stretches, which must be remodeled to promote uridine insertion/deletion. Here we show that the RRM domain of the essential kRNA-editing factor TbRGG2 binds poly(G) and poly(U) RNA and can unfold both. A region C-terminal to the RRM mediates TbRGG2 dimerization, enhancing RNA binding. A RRM-U4 RNA structure reveals a unique RNA-binding mechanism in which the two RRMs of the dimer employ aromatic residues outside the canonical RRM RNA-binding motifs to encase and wrench open the RNA, while backbone atoms specify the uridine bases. Notably, poly(G) RNA is bound via a different binding surface. Thus, these data indicate that TbRGG2 RRM can bind and remodel several RNA substrates suggesting how it might play multiple roles in the kRNA editing process. PubMed: 30544166DOI: 10.1093/nar/gky1259 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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