4ME2
Crystal Structure of THA8 protein from Brachypodium distachyon
Summary for 4ME2
| Entry DOI | 10.2210/pdb4me2/pdb |
| Descriptor | Uncharacterized protein (2 entities in total) |
| Functional Keywords | pentatricopeptide repeat protein, helix-turn-helix repeats, rna binding protein, group ii intron rna binding, chloroplast |
| Biological source | Brachypodium distachyon (Purple false brome) |
| Total number of polymer chains | 1 |
| Total formula weight | 27752.73 |
| Authors | Ke, J.,Chen, R.Z.,Ban, T.,Brunzelle, J.S.,Gu, X.,Melcher, K.,Xu, H.E. (deposition date: 2013-08-24, release date: 2013-10-30, Last modification date: 2024-02-28) |
| Primary citation | Ke, J.,Chen, R.Z.,Ban, T.,Zhou, X.E.,Gu, X.,Tan, M.H.,Chen, C.,Kang, Y.,Brunzelle, J.S.,Zhu, J.K.,Melcher, K.,Xu, H.E. Structural basis for RNA recognition by a dimeric PPR-protein complex. Nat.Struct.Mol.Biol., 20:1377-1382, 2013 Cited by PubMed Abstract: Thylakoid assembly 8 (THA8) is a pentatricopeptide repeat (PPR) RNA-binding protein required for the splicing of the transcript of ycf3, a gene involved in chloroplast thylakoid-membrane biogenesis. Here we report the identification of multiple THA8-binding sites in the ycf3 intron and present crystal structures of Brachypodium distachyon THA8 either free of RNA or bound to two of the identified RNA sites. The apostructure reveals a THA8 monomer with five tandem PPR repeats arranged in a planar fold. The complexes of THA8 bound to the two short RNA fragments surprisingly reveal asymmetric THA8 dimers with the bound RNAs at the dimeric interface. RNA binding induces THA8 dimerization, with a conserved G nucleotide of the bound RNAs making extensive contacts with both monomers. Together, these results establish a new model of RNA recognition by RNA-induced formation of an asymmetric dimer of a PPR protein. PubMed: 24186060DOI: 10.1038/nsmb.2710 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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