4FZV
Crystal structure of the human MTERF4:NSUN4:SAM ternary complex
Summary for 4FZV
Entry DOI | 10.2210/pdb4fzv/pdb |
Descriptor | Putative methyltransferase NSUN4, mTERF domain-containing protein 2, S-ADENOSYLMETHIONINE, ... (6 entities in total) |
Functional Keywords | mterf fold, methyltransferase fold, rrna methyltransferase, mitochondria, transferase |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 2 |
Total formula weight | 68159.72 |
Authors | Guja, K.E.,Yakubovskaya, E.,Mejia, E.,Castano, S.,Hambardjieva, E.,Choi, W.S.,Garcia-Diaz, M. (deposition date: 2012-07-08, release date: 2012-10-03, Last modification date: 2012-11-28) |
Primary citation | Yakubovskaya, E.,Guja, K.E.,Mejia, E.,Castano, S.,Hambardjieva, E.,Choi, W.S.,Garcia-Diaz, M. Structure of the Essential MTERF4:NSUN4 Protein Complex Reveals How an MTERF Protein Collaborates to Facilitate rRNA Modification. Structure, 20:1940-1947, 2012 Cited by PubMed Abstract: MTERF4 is the first MTERF family member shown to bind RNA and plays an essential role as a regulator of ribosomal biogenesis in mammalian mitochondria. It forms a complex with the rRNA methyltransferase NSUN4 and recruits it to the large ribosomal subunit. In this article, we characterize the interaction between both proteins, demonstrate that MTERF4 strongly stimulates the specificity of NSUN4 during in vitro methylation experiments, and present the 2.0 Å resolution crystal structure of the MTERF4:NSUN4 protein complex, lacking 48 residues of the MTERF4 C-terminal acidic tail, bound to S-adenosyl-L-methionine, thus revealing the nature of the interaction between both proteins and the structural conservation of the most divergent of the human MTERF family members. Moreover, the structure suggests a model for RNA binding by the MTERF4:NSUN4 complex, providing insight into the mechanism by which an MTERF family member facilitates rRNA methylation. PubMed: 23022348DOI: 10.1016/j.str.2012.08.027 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9996 Å) |
Structure validation
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