1YJO

Structure of NNQQNY from yeast prion Sup35 with zinc acetate

Summary for 1YJO

• Entry DOI: 10.2210/pdb1yjo/pdb
• Related: 1YJP
• Descriptor: Eukaryotic peptide chain release factor GTP-binding subunit, ZINC ION, ACETIC ACID, ... (4 entities in total)
• Functional Keywords: keywords beta sheet, steric zipper, glutamine zipper, asparagine zipper, protein binding
• Cellular location: Cytoplasm (Probable): P05453
• Total number of polymer chains: 1
• Total formula weight: 905.22

Authors

Nelson, R.,Sawaya, M.R.,Balbirnie, M.,Madsen, A.O.,Riekel, C.,Grothe, R.,Eisenberg, D. (deposition date: 2005-01-15, release date: 2005-06-14, Last modification date: 2024-02-14)

Primary citation

Nelson, R.,Sawaya, M.R.,Balbirnie, M.,Madsen, A.O.,Riekel, C.,Grothe, R.,Eisenberg, D.
Structure of the cross-beta spine of amyloid-like fibrils.
Nature, 435:773-778, 2005

PubMed Abstract: Numerous soluble proteins convert to insoluble amyloid-like fibrils that have common properties. Amyloid fibrils are associated with fatal diseases such as Alzheimer's, and amyloid-like fibrils can be formed in vitro. For the yeast protein Sup35, conversion to amyloid-like fibrils is associated with a transmissible infection akin to that caused by mammalian prions. A seven-residue peptide segment from Sup35 forms amyloid-like fibrils and closely related microcrystals, from which we have determined the atomic structure of the cross-beta spine. It is a double beta-sheet, with each sheet formed from parallel segments stacked in register. Side chains protruding from the two sheets form a dry, tightly self-complementing steric zipper, bonding the sheets. Within each sheet, every segment is bound to its two neighbouring segments through stacks of both backbone and side-chain hydrogen bonds. The structure illuminates the stability of amyloid fibrils, their self-seeding characteristic and their tendency to form polymorphic structures.

PubMed: 15944695
DOI: 10.1038/nature03680

Experimental method

X-RAY DIFFRACTION (1.3 Å)