6E4N

Structure of the T. brucei TbRGG2 RRM domain: apo R3 crystal form

Summary for 6E4N

• Entry DOI: 10.2210/pdb6e4n/pdb
• Descriptor: RNA-binding protein, putative (2 entities in total)
• Functional Keywords: rrm, tbrgg2, krna editing, rna binding, rna binding protein
• Biological source: Trypanosoma brucei
• Total number of polymer chains: 1
• Total formula weight: 7816.77

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

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: 30544166
DOI: 10.1093/nar/gky1259

Experimental method

X-RAY DIFFRACTION (1.801 Å)