5i55 | pdb_00005i55

Crystal Structure of the Virulent PSM-alpha3 Peptide Forming a Cross-alpha amyloid-like Fibril

spinqualitylabelsall models 5i55, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5i55 is a 1 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.45Å Ligands: ACT, MPD, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PSMA3_STAA8 Peptide which can recruit, activate and subsequently lyse human neutrophils, thus eliminating the main cellular defense against infection. Publication Abstract from PubMed Amyloids are ordered protein aggregates, found in all kingdoms of life, and are involved in aggregation diseases as well as in physiological activities. In microbes, functional amyloids are often key virulence determinants, yet the structural basis for their activity remains elusive. We determined the fibril structure and function of the highly toxic, 22-residue phenol-soluble modulin alpha3 (PSMalpha3) peptide secreted by Staphylococcus aureus PSMalpha3 formed elongated fibrils that shared the morphological and tinctorial characteristics of canonical cross-beta eukaryotic amyloids. However, the crystal structure of full-length PSMalpha3, solved de novo at 1.45 angstrom resolution, revealed a distinctive "cross-alpha" amyloid-like architecture, in which amphipathic alpha helices stacked perpendicular to the fibril axis into tight self-associating sheets. The cross-alpha fibrillation of PSMalpha3 facilitated cytotoxicity, suggesting that this assembly mode underlies function in S. aureus. The cytotoxic Staphylococcus aureus PSMalpha3 reveals a cross-alpha amyloid-like fibril.,Tayeb-Fligelman E, Tabachnikov O, Moshe A, Goldshmidt-Tran O, Sawaya MR, Coquelle N, Colletier JP, Landau M Science. 2017 Feb 24;355(6327):831-833. doi: 10.1126/science.aaf4901. PMID:28232575 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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