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8RLH

Neutron structure of hydrogenated hen egg-white lysozyme at room temperature

8RLH の概要
エントリーDOI10.2210/pdb8rlh/pdb
分子名称Lysozyme C, NITRATE ION, ACETATE ION, ... (4 entities in total)
機能のキーワードlysozyme, hydrogenated, room temperature, 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14948.25
構造登録者
Ramos, J.,Laux, V.,Mason, S.A.,Lemee, M.,Bowler, M.,Diederichs, K.,Haertlein, M.,Forsyth, V.T.,Mossou, E.,Larsen, S.,Langkilde, A.E. (登録日: 2024-01-03, 公開日: 2024-11-06, 最終更新日: 2025-01-29)
主引用文献Ramos, J.,Laux, V.,Mason, S.A.,Lemee, M.H.,Bowler, M.W.,Diederichs, K.,Haertlein, M.,Forsyth, V.T.,Mossou, E.,Larsen, S.,Langkilde, A.E.
Structure and dynamics of the active site of hen egg-white lysozyme from atomic resolution neutron crystallography.
Structure, 33:136-148.e3, 2025
Cited by
PubMed Abstract: Hen egg-white lysozyme (HEWL) is a widely used model protein in crystallographic studies and its enzymatic mechanism has been extensively investigated for decades. Despite this, the interaction between the reaction intermediate and the catalytic Asp52, as well as the orientation of Asn44 and Asn46 side chains, remain ambiguous. Here, we report the crystal structures of perdeuterated HEWL and DO buffer-exchanged HEWL from 0.91 and 1.1 Å resolution neutron diffraction data, respectively. These structures were obtained at room temperature and acidic pH, representing the active state of the enzyme. The unambiguous assignment of hydrogen positions based on the neutron scattering length density maps elucidates the roles of Asn44, Asn46, Asn59, and nearby water molecules in the stabilization of Asp52. Additionally, the identification of hydrogen positions reveals unique details of lysozyme's folding, hydrogen (H)/deuterium (D) exchange, and side chain disorder.
PubMed: 39577430
DOI: 10.1016/j.str.2024.10.030
主引用文献が同じPDBエントリー
実験手法
NEUTRON DIFFRACTION (1.1 Å)
構造検証レポート
Validation report summary of 8rlh
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-07-23に公開中

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