4II8

Lysozyme with Benzyl alcohol

4II8 の概要

• エントリーDOI: 10.2210/pdb4ii8/pdb
• 分子名称: Lysozyme C, CHLORIDE ION, SODIUM ION, ... (6 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Gallus gallus (Chicken)
• 細胞内の位置: Secreted: P00698
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14859.19

構造登録者

Sharma, P.,Ashish (登録日: 2012-12-20, 公開日: 2013-12-25, 最終更新日: 2024-10-30)

主引用文献

Sharma, P.,Verma, N.,Singh, P.K.,Korpole, S.,Ashish
Characterization of heat induced spherulites of lysozyme reveals new insight on amyloid initiation
Sci Rep, 6:22475-22475, 2016

PubMed Abstract: Here, we report results obtained during our experiments to visualize how heat transforms globular protein, lysozyme into building block of β-amyloids. Light scattering experiments showed formation of lower order associated species around 50-70 °C followed by rapid cooperativity to β-amyloid fibrils. Interestingly, crystallization drops set at higher temperatures either led to aggregates or spherulites. The latter possess an amorphous β-fibril rich core with thin crystalline needles projecting outwards. Diffraction of the crystalline outgrowths revealed novel dimers and trimers of lysozyme where individual chains were similar to monomer with marginal gain in β-sheet content. Importantly, analysis of Amide I stretching frequencies showed that protein loses its secondary structure at temperatures higher than where we obtained crystals followed by rapid gain in β-sheet content. Interestingly, attempts to use the needles as seeds for more crystals led to "broom-like" fibril formations at the ends. Further, aggregation inhibitors like arginine and benzyl alcohol completely obliterated spherulites formation during crystallization. Refinement of crystals of lysozyme in presence of these molecules showed these small molecules bind to the interfaces of heat associated dimers and trimers. Overall our work concludes that heat induced weakly associated structures of lysozyme are the first step towards its amyloid formation.

PubMed: 26926993
DOI: 10.1038/srep22475

実験手法

X-RAY DIFFRACTION (1.88 Å)