9ZA7
Neurospora crassa polysaccharide monooxygenase 9D dose series - pseudohelix 24 (5.35 MGy)
Summary for 9ZA7
| Entry DOI | 10.2210/pdb9za7/pdb |
| Related | 9Z8O 9Z8P 9Z8Q 9Z8R 9Z8S 9Z8T 9Z8U 9Z8V 9Z8W 9Z8X 9Z8Y 9Z8Z 9Z90 9Z92 9Z93 9Z94 9Z95 9Z96 9Z97 9Z98 9Z99 9ZA5 9ZA6 |
| Descriptor | 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) |
| Functional Keywords | radiation damage, lpmo, photoreduction, polysaccharide monooxygenase, oxidoreductase |
| Biological source | Neurospora crassa |
| Total number of polymer chains | 2 |
| Total formula weight | 48508.98 |
| Authors | |
| Primary citation | 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 Cited by 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: 42517195DOI: 10.1107/S205979832600639X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.1 Å) |
Structure validation
Download full validation report
