7P6M
Hydrogenated refolded hen egg-white lysozyme
7P6M の概要
| エントリーDOI | 10.2210/pdb7p6m/pdb |
| 分子名称 | Lysozyme C, NITRATE ION, ACETATE ION, ... (4 entities in total) |
| 機能のキーワード | lysozyme, hewl, refolded, hydrogenated, recombinant, hydrolase |
| 由来する生物種 | Gallus gallus (Chicken) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 15002.34 |
| 構造登録者 | Ramos, J.,Laux, V.,Haertlein, M.,Forsyth, V.T.,Mossou, E.,Larsen, S.,Langkilde, A.E. (登録日: 2021-07-16, 公開日: 2021-12-22, 最終更新日: 2024-11-20) |
| 主引用文献 | Ramos, J.,Laux, V.,Haertlein, M.,Forsyth, V.T.,Mossou, E.,Larsen, S.,Langkilde, A.E. The impact of folding modes and deuteration on the atomic resolution structure of hen egg-white lysozyme. Acta Crystallogr D Struct Biol, 77:1579-1590, 2021 Cited by PubMed Abstract: The biological function of a protein is intimately related to its structure and dynamics, which in turn are determined by the way in which it has been folded. In vitro refolding is commonly used for the recovery of recombinant proteins that are expressed in the form of inclusion bodies and is of central interest in terms of the folding pathways that occur in vivo. Here, biophysical data are reported for in vitro-refolded hydrogenated hen egg-white lysozyme, in combination with atomic resolution X-ray diffraction analyses, which allowed detailed comparisons with native hydrogenated and refolded perdeuterated lysozyme. Distinct folding modes are observed for the hydrogenated and perdeuterated refolded variants, which are determined by conformational changes to the backbone structure of the Lys97-Gly104 flexible loop. Surprisingly, the structure of the refolded perdeuterated protein is closer to that of native lysozyme than that of the refolded hydrogenated protein. These structural differences suggest that the observed decreases in thermal stability and enzymatic activity in the refolded perdeuterated and hydrogenated proteins are consequences of the macromolecular deuteration effect and of distinct folding dynamics, respectively. These results are discussed in the context of both in vitro and in vivo folding, as well as of lysozyme amyloidogenesis. PubMed: 34866613DOI: 10.1107/S2059798321010950 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (0.89 Å) |
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