6B79

Curved pair of sheets formed from SOD1 residues 28-38 with familial mutation G37R.

Summary for 6B79

• Entry DOI: 10.2210/pdb6b79/pdb
• Descriptor: Superoxide dismutase [Cu-Zn], 7-hydroxy-8-[(E)-phenyldiazenyl]naphthalene-1,3-disulfonic acid (3 entities in total)
• Functional Keywords: amyloid fibril, protein fibril
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 3197.50

Authors

Sangwan, S.,Sawaya, M.R.,Eisenberg, D.S. (deposition date: 2017-10-03, release date: 2018-05-30, Last modification date: 2023-11-15)

Primary citation

Sangwan, S.,Sawaya, M.R.,Murray, K.A.,Hughes, M.P.,Eisenberg, D.S.
Atomic structures of corkscrew-forming segments of SOD1 reveal varied oligomer conformations.
Protein Sci., 27:1231-1242, 2018

PubMed Abstract: The aggregation cascade of disease-related amyloidogenic proteins, terminating in insoluble amyloid fibrils, involves intermediate oligomeric states. The structural and biochemical details of these oligomers have been largely unknown. Here we report crystal structures of variants of the cytotoxic oligomer-forming segment residues 28-38 of the ALS-linked protein, SOD1. The crystal structures reveal three different architectures: corkscrew oligomeric structure, nontwisting curved sheet structure and a steric zipper proto-filament structure. Our work highlights the polymorphism of the segment 28-38 of SOD1 and identifies the molecular features of amyloidogenic entities.

PubMed: 29453800
DOI: 10.1002/pro.3391

Experimental method

X-RAY DIFFRACTION (1.8 Å)