9h1m | pdb_00009h1m

Recombinant ferric horseradish peroxidase C1A

spinqualitylabelsall models 9h1m, resolution 1.63Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9h1m is a 1 chain structure with sequence from Armoracia rusticana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.63Å Ligands: 2HP, CA, EDO, HEM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PER1A_ARMRU Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. Publication Abstract from PubMed Horseradish peroxidase (HRP), isolated from horseradish roots, is heavily glycosylated, making it difficult to crystallize. In this work, we produced recombinant HRP in E. coli and obtained an X-ray structure of the ferric enzyme at 1.63 A resolution. The structure shows that the recombinant HRP contains four disulphide bonds and two calcium ions, which are highly conserved in class III peroxidase enzymes. The heme active site contains histidine residues at the proximal (His 170) and distal (His 42) positions, and an active site arginine (Arg 38). Surprisingly, an ethylene glycol molecule was identified in the active site, forming hydrogen bonds with His 42 and Arg 38 at the delta-heme edge. The high yields obtained from the recombinant expression system, and the successful crystallization of the enzyme pave the way for new structural studies in the future. Crystal structure of ferric recombinant horseradish peroxidase.,Nesa ML, Mandal SK, Toelzer C, Humer D, Moody PCE, Berger I, Spadiut O, Raven EL J Biol Inorg Chem. 2025 Mar 7. doi: 10.1007/s00775-025-02103-2. PMID:40053124 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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