Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Myeloperoxidase transforms chromatin into neutrophil extracellular traps.
Journal, issue, pages	Nature, Vol. 647, Issue 8090, Page 747-756, Year 2025
Publish date	Sep 17, 2025
Authors	Garth Lawrence Burn / Tobias Raisch / Sebastian Tacke / Moritz Winkler / Daniel Prumbaum / Stephanie Thee / Niclas Gimber / Stefan Raunser / Arturo Zychlinsky /
PubMed Abstract	Neutrophils, the most abundant and biotoxic immune cells, extrude nuclear DNA into the extracellular space to maintain homeostasis. Termed neutrophil extracellular traps (NETs), these protein- ...Neutrophils, the most abundant and biotoxic immune cells, extrude nuclear DNA into the extracellular space to maintain homeostasis. Termed neutrophil extracellular traps (NETs), these protein-modified and decondensed extracellular DNA scaffolds control infection and are involved in coagulation, autoimmunity and cancer. Here we show how myeloperoxidase (MPO), a highly expressed neutrophil protein, disassembles nucleosomes, thereby facilitating NET formation, yet also binds stably to NETs extracellularly. We describe how the oligomeric status of MPO governs both outcomes. MPO dimers interact with nucleosomal DNA using one protomer and concurrently dock into the nucleosome acidic patch with the other protomer. As a consequence, dimeric MPO displaces DNA from the core complex, culminating in nucleosome disassembly. On the other hand, MPO monomers stably interact with the nucleosome acidic patch without making concomitant DNA contacts, explaining how monomeric MPO binds to and licences NETs to confer hypohalous acid production in the extracellular space. Our data demonstrate that the binding of MPO to chromatin is governed by specific molecular interactions that transform chromatin into a non-replicative, non-encoding state that offers new biological functions in a cell-free manner. We propose that MPO is, to our knowledge, the first member of a class of proteins that convert chromatin into an immune effector.
External links	Nature / PubMed:40963017 / PubMed Central
Methods	EM (single particle)
Resolution	2.79 - 3.99 Å
Structure data	51295 9gen EMDB-51295, PDB-9gen: Recombinant Myeloperoxidase bound to nucleosome core particle Method: EM (single particle) / Resolution: 3.76 Å 51296 9geo EMDB-51296, PDB-9geo: Nucleosome core particle Method: EM (single particle) / Resolution: 2.79 Å 51297 9gep EMDB-51297, PDB-9gep: Native monomeric Myeloperoxidase bound to nucleosome core particle Method: EM (single particle) / Resolution: 2.89 Å EMDB-51298: Native dimeric Myeloperoxidase bound to nucleosome core particle; nucleosome focused map Method: EM (single particle) / Resolution: 3.01 Å EMDB-51299: Native dimeric Myeloperoxidase bound to nucleosome core particle; MPO focused map Method: EM (single particle) / Resolution: 2.98 Å EMDB-51300: Native dimeric Myeloperoxidase bound to nucleosome core particle; consensus map Method: EM (single particle) / Resolution: 3.12 Å 51301 9geq EMDB-51301, PDB-9geq: Native dimeric Myeloperoxidase bound to nucleosome core particle; composite map Method: EM (single particle) / Resolution: 3.12 Å EMDB-51302: Native dimeric Myeloperoxidase bound to nucleosome core particle, intermediate state, nucleosome focused map Method: EM (single particle) / Resolution: 3.52 Å EMDB-51303: Native dimeric Myeloperoxidase bound to nucleosome core particle, intermediate state, map focused on MPO Method: EM (single particle) / Resolution: 3.87 Å EMDB-51304: Native dimeric Myeloperoxidase bound to nucleosome core particle, intermediate state, consensus map Method: EM (single particle) / Resolution: 3.58 Å 51305 9ger EMDB-51305, PDB-9ger: Native dimeric Myeloperoxidase bound to nucleosome core particle, intermediate state; composite map Method: EM (single particle) / Resolution: 3.58 Å EMDB-51306: Native monomeric Myeloperoxidase bound to nucleosome core particle, late time point Method: EM (single particle) / Resolution: 3.99 Å 52865 9ihd EMDB-52865, PDB-9ihd: Nucleosome core particle bound by one molecule of DTT-reduced native monomeric myeloperoxidase Method: EM (single particle) / Resolution: 2.97 Å 52866 9ihe EMDB-52866, PDB-9ihe: Nucleosome core particle bound by two molecules of DTT-reduced native monomeric myeloperoxidase Method: EM (single particle) / Resolution: 2.95 Å EMDB-52867: Nucleosome core particle bound by one monomer and one dimer of of DTT-reduced native myeloperoxidase; map focused on nucleosome/MPO monomer Method: EM (single particle) / Resolution: 3.13 Å EMDB-52868: Nucleosome core particle bound by one monomer and one dimer of of DTT-reduced native myeloperoxidase; map focused on MPO dimer Method: EM (single particle) / Resolution: 3.17 Å EMDB-52869: Nucleosome core particle bound by one monomer and one dimer of of DTT-reduced native myeloperoxidase; consensus map Method: EM (single particle) / Resolution: 3.16 Å 52870 9ihf EMDB-52870, PDB-9ihf: Nucleosome core particle bound by one monomer and one dimer of of DTT-reduced native myeloperoxidase Method: EM (single particle) / Resolution: 3.16 Å
Chemicals	ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose ChemComp-HOH: WATER ChemComp-HEM: PROTOPORPHYRIN IX CONTAINING FE ChemComp-CL: Unknown entry ChemComp-CA: Unknown entry
Source	homo sapiens (human) xenopus laevis (African clawed frog) synthetic construct (others)
Keywords	IMMUNE SYSTEM / Peroxidase / innate immunity / histone / acidic patch / NUCLEAR PROTEIN / NETs