View source for 21rn


==Cryo-EM structure of mouse myeloperoxidase in complex with Fab fragments of antibodies mAb-A24 and mAb-A46==
<StructureSection load='21rn' size='340' side='right'caption='[[21rn]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[21rn]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=21RN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=21RN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=21rn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=21rn OCA], [https://pdbe.org/21rn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=21rn RCSB], [https://www.ebi.ac.uk/pdbsum/21rn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=21rn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PERM_MOUSE PERM_MOUSE] Peroxidase that plays a central role in the host defense system of polymorphonuclear leukocytes by mediating both (1) formation of neutrophil extracellular trap (NETs) and (2) microbicidal activity (PubMed:10085024, PubMed:11593004, PubMed:23306200). Promotes NET formation by mediating chromatin disassembly: translocates to the nucleus and specifically binds to nucleosomes, both as monomer and homodimer, leading to nucleosome unstacking and initial chromatin decondensation (By similarity). Homodimers clash with one end of the nucleosomal DNA, leading to DNA unwrapping, initiating complete disassembly of nucleosomes and chromatin transformation into NETs in an ATP-independent manner (By similarity). NETs, which are mainly composed of DNA fibers and globular proteins, are then extruded into the extracellular space by neutrophils to trap pathogens and release antimicrobial proteins to destroy them (By similarity). Participates to the microbicidal activity against a wide range of organisms by acting as a peroxidase that catalyzes the formation of oxidants in presence of hydrogen peroxide (PubMed:11593004). Mediates the formation of hypohalous acids, mainly hypochlorous acid (HOCl) in physiologic situations, that greatly enhance polymorphonuclear leukocyte microbicidal activity (PubMed:11593004, PubMed:23306200). In addition to hypochlorous acid, catalyzes formation of hypobromous acid (HOBr), hypoiodous acid (HOI) and hypothiocyanous acid (HOSCN) (By similarity). Also catalyzes oxidation of nitrite into the highly reactive nitrogen dioxide radical (By similarity). Formation of oxidants are widely believed to be responsible for much of the anti-bactericidal activity of neutrophils (By similarity). Oxidants, such as hypochlorous acid or nitrogen dioxide radical, can also oxidize amino acid residues on proteins and generate chlorination and nitration post-translational modifications, respectively (By similarity). Chlorination and nitration of the lipid-free form of APOA1 impairs cholesterol transport (By similarity). Superoxides generated by MPO can also promote dioxygenation of tryptophan residues on proteins (By similarity). Also able to oxidize melatonin into N1-acetyl-N2-formyl-5-methoxykynuramine either in presence of hydrogen peroxide or superoxide (By similarity). Oxidizes urate into 5-hydroxyisourate (By similarity). Functions as a nitric oxide (NO) oxidase during inflammation, by catalytically consuming NO, impairing NO's ability to maintain vascular tone and function (By similarity). May also mediate the proteolytic cleavage of alpha-1-microglobulin to form t-alpha-1-microglobulin, which potently inhibits oxidation of low-density lipoprotein particles and limits vascular damage (By similarity).[UniProtKB:P05164]<ref>PMID:10085024</ref> <ref>PMID:11593004</ref> <ref>PMID:23306200</ref>   Light chain of the mature myeloperoxidase.[UniProtKB:P05164]  Heavy chain of the mature myeloperoxidase.[UniProtKB:P05164]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Fujii T]]
[[Category: Irie M]]
[[Category: Torizawa T]]