7N8R

FGTGFG segment from the Nucleoporin p54, residues 63-68

Summary for 7N8R

• Entry DOI: 10.2210/pdb7n8r/pdb
• Descriptor: FGTGFG segment from the Nucleoporin p54, residues 63-68, trifluoroacetic acid (3 entities in total)
• Functional Keywords: amyloid-like fibril, protein fibril
• Biological source: Homo sapiens
• Total number of polymer chains: 2
• Total formula weight: 1283.27

Authors

Hughes, M.P.,Sawaya, M.R.,Eisenberg, D.S. (deposition date: 2021-06-15, release date: 2022-02-16, Last modification date: 2024-05-22)

Primary citation

Murray, K.A.,Evans, D.,Hughes, M.P.,Sawaya, M.R.,Hu, C.J.,Houk, K.N.,Eisenberg, D.
Extended beta-Strands Contribute to Reversible Amyloid Formation.
Acs Nano, 16:2154-2163, 2022

PubMed Abstract: The assembly of proteins into fibrillar amyloid structures was once considered to be pathologic and essentially irreversible. Recent studies reveal amyloid-like structures that form reversibly, derived from protein low-complexity domains which function in cellular metabolism. Here, by comparing atomic-level structures of reversible and irreversible amyloid fibrils, we find that the β-sheets of reversible fibrils are enriched in flattened (as opposed to pleated) β-sheets formed by stacking of extended β-strands. Quantum mechanical calculations show that glycine residues favor extended β-strands which may be stabilized by intraresidue interactions between the amide proton and the carbonyl oxygen, known as C5 hydrogen-bonds. Larger residue side chains favor shorter strands and pleated sheets. These findings highlight a structural element that may regulate reversible amyloid assembly.

PubMed: 35132852
DOI: 10.1021/acsnano.1c08043

Experimental method

X-RAY DIFFRACTION (1.2 Å)