7qv5

Amyloid fibril from the antimicrobial peptide uperin 3.5

spinqualitylabelsall models 7qv5, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7qv5 is a 27 chain structure with sequence from Uperoleia mjobergii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3Å Ligands: NH2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function UPE35_UPEMJ Publication Abstract from PubMed The amyloid-antimicrobial link hypothesis is based on antimicrobial properties found in human amyloids involved in neurodegenerative and systemic diseases, along with amyloidal structural properties found in antimicrobial peptides (AMPs). Supporting this hypothesis, we here determined the fibril structure of two AMPs from amphibians, uperin 3.5 and aurein 3.3, by cryogenic electron microscopy (cryo-EM), revealing amyloid cross-beta fibrils of mated beta-sheets at atomic resolution. Uperin 3.5 formed a 3-blade symmetrical propeller of nine peptides per fibril layer including tight beta-sheet interfaces. This cross-beta cryo-EM structure complements the cross-alpha fibril conformation previously determined by crystallography, substantiating a secondary structure switch mechanism of uperin 3.5. The aurein 3.3 arrangement consisted of six peptides per fibril layer, all showing kinked beta-sheets allowing a rounded compactness of the fibril. The kinked beta-sheets are similar to LARKS (Low-complexity, Amyloid-like, Reversible, Kinked Segments) found in human functional amyloids. The Cryo-EM structures of two amphibian antimicrobial cross-beta amyloid fibrils.,Bucker R, Seuring C, Cazey C, Veith K, Garcia-Alai M, Grunewald K, Landau M Nat Commun. 2022 Jul 27;13(1):4356. doi: 10.1038/s41467-022-32039-z. PMID:35896552 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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