8RLH
Neutron structure of hydrogenated hen egg-white lysozyme at room temperature
8RLH の概要
エントリーDOI | 10.2210/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: 39577430DOI: 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) |
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