5XSG
Ultrahigh resolution structure of FUS (37-42) SYSGYS determined by MicroED
Summary for 5XSG
| Entry DOI | 10.2210/pdb5xsg/pdb |
| Descriptor | RNA-binding protein FUS (2 entities in total) |
| Functional Keywords | cross-coil amyloid fibril, fus low complexity domain, reversible amyloid fibril, rna granule assembly, rna binding protein |
| Biological source | Homo sapiens (Human) |
| Cellular location | Nucleus : P35637 |
| Total number of polymer chains | 1 |
| Total formula weight | 662.65 |
| Authors | |
| Primary citation | Luo, F.,Gui, X.,Zhou, H.,Gu, J.,Li, Y.,Liu, X.,Zhao, M.,Li, D.,Li, X.,Liu, C. Atomic structures of FUS LC domain segments reveal bases for reversible amyloid fibril formation. Nat. Struct. Mol. Biol., 25:341-346, 2018 Cited by PubMed Abstract: Thermostable cross-β structures are characteristic of pathological amyloid fibrils, but these structures cannot explain the reversible nature of fibrils formed by RNA-binding proteins such as fused in sarcoma (FUS), involved in RNA granule assembly. Here, we find that two tandem (S/G)Y(S/G) motifs of the human FUS low-complexity domain (FUS LC) form reversible fibrils in a temperature- and phosphorylation-dependent manner. We named these motifs reversible amyloid cores, or RAC1 and RAC2, and determined their atomic structures in fibrillar forms, using microelectron and X-ray diffraction techniques. The RAC1 structure features an ordered-coil fibril spine rather than the extended β-strand typical of amyloids. Ser42, a phosphorylation site of FUS, is critical in the maintenance of the ordered-coil structure, which explains how phosphorylation controls fibril formation. The RAC2 structure shows a labile fibril spine with a wet interface. These structures illuminate the mechanism of reversible fibril formation and dynamic assembly of RNA granules. PubMed: 29610493DOI: 10.1038/s41594-018-0050-8 PDB entries with the same primary citation |
| Experimental method | ELECTRON CRYSTALLOGRAPHY (0.73 Å) |
Structure validation
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