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TitleAtomic structures of low-complexity protein segments reveal kinked β sheets that assemble networks.
Journal, issue, pagesScience, Vol. 359, Issue 6376, Page 698-701, Year 2018
Publish dateFeb 9, 2018
AuthorsMichael P Hughes / Michael R Sawaya / David R Boyer / Lukasz Goldschmidt / Jose A Rodriguez / Duilio Cascio / Lisa Chong / Tamir Gonen / David S Eisenberg /
PubMed AbstractSubcellular 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. ...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.
External linksScience / PubMed:29439243 / PubMed Central
MethodsX-ray diffraction / EM (electron crystallography)
Resolution0.9 - 1.1 Å
Structure data

PDB-6bwz:
SYSGYS from low-complexity domain of FUS, residues 37-42
Method: X-RAY DIFFRACTION / Resolution: 1.1 Å

PDB-6bxv:
SYSSYGQS from low-complexity domain of FUS, residues 54-61
Method: X-RAY DIFFRACTION / Resolution: 1.1 Å

PDB-6bxx:
GYNGFG from low-complexity domain of hnRNPA1, residues 243-248
Method: X-RAY DIFFRACTION / Resolution: 1.1 Å

PDB-6bzm:
GFGNFGTS from low-complexity/FG repeat domain of Nup98, residues 116-123
Method: ELECTRON CRYSTALLOGRAPHY / Resolution: 0.9 Å

PDB-6bzp:
STGGYG from low-complexity domain of FUS, residues 77-82
Method: ELECTRON CRYSTALLOGRAPHY / Resolution: 1.1 Å

Chemicals

ChemComp-HOH:
WATER / Water

ChemComp-TOE:
2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXYL

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / Amyloid / LARKS / Reversible-amyloid / low-complexity / FG repeat

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