5XRR

Crystal structure of FUS (54-59) SYSSYG

Summary for 5XRR

• Entry DOI: 10.2210/pdb5xrr/pdb
• Descriptor: RNA-binding protein FUS, ZINC ION (3 entities in total)
• Functional Keywords: reversible amyloid, hydrous amyloid fibril spine, low complexity domain, rna granule assembly, rna binding protein
• Biological source: Homo sapiens (Human)
• Cellular location: Nucleus : P35637
• Total number of polymer chains: 1
• Total formula weight: 728.06

Authors

Zhao, M.,Gui, X.,Li, D.,Liu, C. (deposition date: 2017-06-09, release date: 2018-04-04, Last modification date: 2024-03-27)

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

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: 29610493
DOI: 10.1038/s41594-018-0050-8

Experimental method

X-RAY DIFFRACTION (1.503 Å)