6BWZ

SYSGYS from low-complexity domain of FUS, residues 37-42

Summary for 6BWZ

• Entry DOI: 10.2210/pdb6bwz/pdb
• Descriptor: SYSGYS peptide from low-complexity domain of FUS (2 entities in total)
• Functional Keywords: amyloid, larks, reversible-amyloid, low-complexity, protein fibril
• Biological source: Homo sapiens
• Total number of polymer chains: 1
• Total formula weight: 662.65

Authors

Hughes, M.P.,Rodriguez, J.A.,Sawaya, M.R.,Cascio, D.,Tamir, G.,Eisenberg, D.S. (deposition date: 2017-12-15, release date: 2018-04-04, Last modification date: 2023-10-04)

Primary citation

Hughes, M.P.,Sawaya, M.R.,Boyer, D.R.,Goldschmidt, L.,Rodriguez, J.A.,Cascio, D.,Chong, L.,Gonen, T.,Eisenberg, D.S.
Atomic structures of low-complexity protein segments reveal kinked beta sheets that assemble networks.
Science, 359:698-701, 2018

PubMed Abstract: Subcellular membraneless assemblies are a reinvigorated area of study in biology, with spirited scientific discussions on the forces between the low-complexity protein domains within these assemblies. To illuminate these forces, we determined the atomic structures of five segments from protein low-complexity domains associated with membraneless assemblies. Their common structural feature is the stacking of segments into kinked β sheets that pair into protofilaments. Unlike steric zippers of amyloid fibrils, the kinked sheets interact weakly through polar atoms and aromatic side chains. By computationally threading the human proteome on our kinked structures, we identified hundreds of low-complexity segments potentially capable of forming such interactions. These segments are found in proteins as diverse as RNA binders, nuclear pore proteins, and keratins, which are known to form networks and localize to membraneless assemblies.

PubMed: 29439243
DOI: 10.1126/science.aan6398

Experimental method

X-RAY DIFFRACTION (1.1 Å)