7S02
Crystal structure of FBF-2 in complex with LST-1 site A peptide and FBE RNA
Summary for 7S02
| Entry DOI | 10.2210/pdb7s02/pdb |
| Related | 7RZZ |
| Descriptor | Fem-3 mRNA-binding factor 2, FBE RNA, Lateral Signaling Target, ... (6 entities in total) |
| Functional Keywords | pumilio rna-binding proteins, rna binding protein |
| Biological source | Caenorhabditis elegans More |
| Total number of polymer chains | 3 |
| Total formula weight | 53984.47 |
| Authors | Qiu, C.,Hall, T.M.T. (deposition date: 2021-08-28, release date: 2021-12-29, Last modification date: 2023-10-18) |
| Primary citation | Qiu, C.,Wine, R.N.,Campbell, Z.T.,Hall, T.M.T. Bipartite interaction sites differentially modulate RNA-binding affinity of a protein complex essential for germline stem cell self-renewal. Nucleic Acids Res., 50:536-548, 2022 Cited by PubMed Abstract: In C. elegans, PUF proteins promote germline stem cell self-renewal. Their functions hinge on partnerships with two proteins that are redundantly required for stem cell maintenance. Here we focus on understanding how the essential partner protein, LST-1, modulates mRNA regulation by the PUF protein, FBF-2. LST-1 contains two nonidentical sites of interaction with FBF-2, LST-1 A and B. Our crystal structures of complexes of FBF-2, LST-1 A, and RNA visualize how FBF-2 associates with LST-1 A versus LST-1 B. One commonality is that FBF-2 contacts the conserved lysine and leucine side chains in the KxxL motifs in LST-1 A and B. A key difference is that FBF-2 forms unique contacts with regions N- and C-terminal to the KxxL motif. Consequently, LST-1 A does not modulate the RNA-binding affinity of FBF-2, whereas LST-1 B decreases RNA-binding affinity of FBF-2. The N-terminal region of LST-1 B, which binds near the 5' end of RNA elements, is essential to modulate FBF-2 RNA-binding affinity, while the C-terminal residues of LST-1 B contribute strong binding affinity to FBF-2. We conclude that LST-1 has the potential to impact which mRNAs are regulated depending on the precise nature of engagement through its functionally distinct FBF binding sites. PubMed: 34908132DOI: 10.1093/nar/gkab1220 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.34 Å) |
Structure validation
Download full validation report
