9bnh

X-ray Crystal Structure of Cu-TZ4H tryptophan Zipper Metallo-Peptide

spinqualitylabelsall models 9bnh, resolution 1.12Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9bnh is a 2 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 1.12Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Metal binding to beta-sheets occurs in many metalloproteins and is also implicated in the pathology of Alzheimer's disease. De novo designed metallo-beta-sheets have been pursued as models and mimics of these proteins. However, no crystal structures of canonical beta-sheet metallopeptides have yet been obtained, in stark contrast to many examples for a-helical metallopeptides, leading to a poor understanding for their chemistry. To address this, we have engineered tryptophan zippers, stable 12-residue beta-sheet peptides, to bind Cu(II) ions and obtained crystal structures through single crystal X-ray diffraction (SC-XRD). We find that metal binding triggers several unexpected supramolecular assemblies that demonstrate the range of higher-order structures available to metallo-beta-sheets. Overall, these findings underscore the importance of crystallography in elucidating the rich structural landscape of metallo-beta-sheet peptides. Crystallography reveals metal-triggered restructuring of beta-hairpins.,Dang VT, Engineer A, McElheny D, Drena A, Telser J, Tomczak K, Nguyen AI Chemistry. 2024 Aug 16:e202402101. doi: 10.1002/chem.202402101. PMID:39152095 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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