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TitleThe structure of a β-microglobulin fibril suggests a molecular basis for its amyloid polymorphism.
Journal, issue, pagesNat Commun, Vol. 9, Issue 1, Page 4517, Year 2018
Publish dateOct 30, 2018
AuthorsMatthew G Iadanza / Robert Silvers / Joshua Boardman / Hugh I Smith / Theodoros K Karamanos / Galia T Debelouchina / Yongchao Su / Robert G Griffin / Neil A Ranson / Sheena E Radford /
PubMed AbstractAll amyloid fibrils contain a cross-β fold. How this structure differs in fibrils formed from proteins associated with different diseases remains unclear. Here, we combine cryo-EM and MAS-NMR to ...All amyloid fibrils contain a cross-β fold. How this structure differs in fibrils formed from proteins associated with different diseases remains unclear. Here, we combine cryo-EM and MAS-NMR to determine the structure of an amyloid fibril formed in vitro from β-microglobulin (βm), the culprit protein of dialysis-related amyloidosis. The fibril is composed of two identical protofilaments assembled from subunits that do not share βm's native tertiary fold, but are formed from similar β-strands. The fibrils share motifs with other amyloid fibrils, but also contain unique features including π-stacking interactions perpendicular to the fibril axis and an intramolecular disulfide that stabilises the subunit fold. We also describe a structural model for a second fibril morphology and show that it is built from the same subunit fold. The results provide insights into the mechanisms of fibril formation and the commonalities and differences within the amyloid fold in different protein sequences.
External linksNat Commun / PubMed:30375379 / PubMed Central
MethodsEM (helical sym.)
Resolution3.975 - 6.69 Å
Structure data

0014

6gk3

EMDB-0014, PDB-6gk3:
Two protofilament beta-2-microglobulin amyloid fibril
Method: EM (helical sym.) / Resolution: 3.975 Å

EMDB-0021:
Single protofilament beta-2-microglobulin amyloid fibril
Method: EM (helical sym.) / Resolution: 6.69 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / amyloid / b2m

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