Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

7P6M

Hydrogenated refolded hen egg-white lysozyme

7P6M の概要
エントリーDOI10.2210/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: 34866613
DOI: 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)
構造検証レポート
Validation report summary of 7p6m
検証レポート(詳細版)ダウンロードをダウンロード

252456

件を2026-04-22に公開中

PDB statisticsPDBj update infoContact PDBjnumon