9h1m
From Proteopedia
Recombinant ferric horseradish peroxidase C1A
Structural highlights
FunctionPER1A_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 PubMedHorseradish 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Armoracia rusticana | Large Structures | Berger I | Humer D | Mandal SK | Moody PCE | Nesa ML | Raven EL | Spadiut O | Toelzer C