5vsg

Fibrils of the super helical repeat peptide, SHR-FF, grown at elevated temperature

spinqualitylabelsall models 5vsg, resolution 1.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5vsg is a 1 chain structure with sequence from Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.1Å Ligands: AIB Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The ensemble of native, folded state was once considered to represent the global energy minimum of a given protein sequence. More recently, the discovery of the cross-beta amyloid state revealed that deeper energy minima exist, often associated with pathogenic, fibrillar deposits, when the concentration of proteins reaches a critical value. Fortunately, a sizable energy barrier impedes the conversion from native to pathogenic states. However, little is known about the structure of the related transition state. In addition, there are indications of polymorphism in the amyloidogenic process. Here, we report the first evidence of the conversion of metastable cross-alpha-helical crystals to thermodynamically stable cross-beta-sheet-like fibrils by a de novo designed heptapeptide. Furthermore, for the first time, we demonstrate at atomic resolution that the flip of a peptide plane from a type I to a type II' turn facilitates transformation to cross-beta structure and assembly of a dry steric zipper. This study establishes the potential of a peptide turn, a common protein secondary structure, to serve as a principal gatekeeper between a native metastable folded state and the amyloid state. Transition of Metastable Cross-alpha Crystals into Cross-beta Fibrils by beta-Turn Flipping.,Mondal S, Jacoby G, Sawaya MR, Arnon ZA, Adler-Abramovich L, Rehak P, Vukovic L, Shimon LJW, Kral P, Beck R, Gazit E J Am Chem Soc. 2019 Jan 9;141(1):363-369. doi: 10.1021/jacs.8b10289. Epub 2018, Dec 26. PMID:30532955 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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