9ZAI

Neurospora crassa polysaccharide monooxygenase 9D dose series - pseudohelix 34 (7.82 MGy)

9ZAI の概要

• エントリーDOI: 10.2210/pdb9zai/pdb
• 関連するPDBエントリー: 9Z8O 9Z8P 9Z8Q 9Z8R 9Z8S 9Z8T 9Z8U 9Z8V 9Z8W 9Z8X 9Z8Y 9Z8Z 9Z90 9Z92 9Z93 9Z94 9Z95 9Z96 9Z97 9Z98 9Z99 9ZA5 9ZA6 9ZA7 9ZA8 9ZA9 9ZAA 9ZAB 9ZAC 9ZAD 9ZAE 9ZAF 9ZAH
• 分子名称: Lytic polysaccharide monooxygenase NCU01050, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total)
• 機能のキーワード: radiation damage, lpmo, photoreduction, polysaccharide monooxygenase, oxidoreductase
• 由来する生物種: Neurospora crassa
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48508.98

構造登録者

Miller, S.A.,O'Dell, W.B.,Meilleur, F. (登録日: 2025-11-19, 公開日: 2026-08-12)

主引用文献

Miller, S.A.,O'Dell, W.B.,Meilleur, F.
Dose-dependent structural and electron-density features in the lytic polysaccharide monooxygenase NcAA9D.
Acta Crystallogr D Struct Biol, 2026

PubMed Abstract: Structural studies of copper-containing lytic polysaccharide monooxygenases (LPMOs) by X-ray crystallography are often complicated by radiation damage. In this study, we analyze a series of 36 X-ray crystal structures of NcAA9D, a Neurospora crassa AA9-family LPMO, determined from data collected at cryogenic temperature from a single crystal to investigate the progressive effects of radiation damage at the active site of this enzyme. We report new insights into the dose-dependence of active-site geometry in LPMOs and utilize the unique pre-bound dioxygen site of NcAA9D to analyze the impact of X-ray dose on the electron density of this species. It is well established that photoreduction of the LPMO active-site copper(II) leads to expulsion of its water ligands. We further characterize this displacement and the corresponding electron-density smearing, a phenomenon that can lead to the erroneous modeling of copper-bound dioxygen species. These findings suggest that radiation-dose series collected from a single crystal provide invaluable data to support unambiguous assignment of radiation-sensitive intermediates at the active site of LPMOs and other radiation-sensitive redox enzymes.

PubMed: 42517195
DOI: 10.1107/S205979832600639X

実験手法

X-RAY DIFFRACTION (1.1 Å)