5TD6

C. elegans FOG-3 BTG/Tob domain - H47N, C117A

Summary for 5TD6

• Entry DOI: 10.2210/pdb5td6/pdb
• Descriptor: FOG-3 protein, SULFATE ION (3 entities in total)
• Functional Keywords: btg/tob, polymer, rna binding, rna binding protein
• Biological source: Caenorhabditis elegans
• Total number of polymer chains: 2
• Total formula weight: 32528.72

Authors

Aoki, S.T.,Bingman, C.A.,Wickens, M.,Kimble, J.E. (deposition date: 2016-09-17, release date: 2017-09-20, Last modification date: 2023-10-04)

Primary citation

Aoki, S.T.,Porter, D.F.,Prasad, A.,Wickens, M.,Bingman, C.A.,Kimble, J.
An RNA-Binding Multimer Specifies Nematode Sperm Fate.
Cell Rep, 23:3769-3775, 2018

PubMed Abstract: FOG-3 is a master regulator of sperm fate in Caenorhabditis elegans and homologous to Tob/BTG proteins, which in mammals are monomeric adaptors that recruit enzymes to RNA binding proteins. Here, we determine the FOG-3 crystal structure and in vitro demonstrate that FOG-3 forms dimers that can multimerize. The FOG-3 multimeric structure has a basic surface potential, suggestive of binding nucleic acid. Consistent with that prediction, FOG-3 binds directly to nearly 1,000 RNAs in nematode spermatogenic germ cells. Most binding is to the 3' UTR, and most targets (94%) are oogenic mRNAs, even though assayed in spermatogenic cells. When tethered to a reporter mRNA, FOG-3 represses its expression. Together these findings elucidate the molecular mechanism of sperm fate specification and reveal the evolution of a protein from monomeric to multimeric form with acquisition of a distinct mode of mRNA repression.

PubMed: 29949762
DOI: 10.1016/j.celrep.2018.05.095

Experimental method

X-RAY DIFFRACTION (2.034 Å)