6J486J48 の概要
| エントリーDOI | 10.2210/pdb6j48/pdb |
| 分子名称 | Outer surface protein A, TETRAETHYLENE GLYCOL (3 entities in total) |
| 機能のキーワード | beta-sheet, de novo protein, lipid binding protein |
| 由来する生物種 | Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 26739.87 |
| 構造登録者 | |
| 主引用文献 | Hori, Y.,Fujiwara, H.,Fujiwara, W.,Makabe, K. Grafting a short chameleon sequence from alpha B crystallin into a beta-sheet scaffold protein. Proteins, 87:416-424, 2019 Cited by PubMed Abstract: Many protein and peptide sequences are self-assembled into β-sheet-rich fibrous structures called amyloids. Their atomic details provide insights into fundamental knowledge related to amyloid diseases. To study the detailed structure of the amyloid, we have developed a model system that mimics the self-assembling process of the amyloid within a water-soluble protein, termed peptide self-assembly mimic (PSAM). PSAM enables capturing of a peptide sequence within a water-soluble protein, thus making structural and energetics-related studies possible. In this work, we extend our PSAM approach to a naturally occurring chameleon sequence from αB crystallin. We chose "Val-Leu-Gly-Asp-Val (VLGDV)", a five amino-acid sequence, which forms a β-turn in the native structure and a β-barrel in the amyloid oligomer cylindrin, as a grafting sequence to the PSAM scaffold. The crystal structure revealed that the sequence grafting induced β-sheet bending at the grafted site. We further investigated the role of the central glycine residue and found that its role in the β-sheet bending is dependent on the neighboring residues. The ability of PSAM to observe the structural alterations induced by the grafted sequence provides an opportunity to evaluate the structural impact of a sequence from the peptide self-assembly. PubMed: 30684364DOI: 10.1002/prot.25663 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.201 Å) |
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