1FHF

THE STRUCTURE OF SOYBEAN PEROXIDASE

Summary for 1FHF

• Entry DOI: 10.2210/pdb1fhf/pdb
• Descriptor: SEED COAT PEROXIDASE, CALCIUM ION, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total)
• Functional Keywords: oxidoreductase
• Biological source: Glycine max (soybean)
• Cellular location: Secreted : O22443
• Total number of polymer chains: 3
• Total formula weight: 102236.67

Authors

Henriksen, A.,Mirza, O.,Indiana, C.,Welinder, K.,Teilum, K.,Gajhede, M. (deposition date: 2000-08-01, release date: 2001-02-14, Last modification date: 2024-10-30)

Primary citation

Henriksen, A.,Mirza, O.,Indiani, C.,Teilum, K.,Smulevich, G.,Welinder, K.G.,Gajhede, M.
Structure of soybean seed coat peroxidase: a plant peroxidase with unusual stability and haem-apoprotein interactions.
Protein Sci., 10:108-115, 2001

PubMed Abstract: Soybean seed coat peroxidase (SBP) is a peroxidase with extraordinary stability and catalytic properties. It belongs to the family of class III plant peroxidases that can oxidize a wide variety of organic and inorganic substrates using hydrogen peroxide. Because the plant enzyme is a heterogeneous glycoprotein, SBP was produced recombinant in Escherichia coli for the present crystallographic study. The three-dimensional structure of SBP shows a bound tris(hydroxymethyl)aminomethane molecule (TRIS). This TRIS molecule has hydrogen bonds to active site residues corresponding to the residues that interact with the small phenolic substrate ferulic acid in the horseradish peroxidase C (HRPC):ferulic acid complex. TRIS is positioned in what has been described as a secondary substrate-binding site in HRPC, and the structure of the SBP:TRIS complex indicates that this secondary substrate-binding site could be of functional importance. SBP has one of the most solvent accessible delta-meso haem edge (the site of electron transfer from reducing substrates to the enzymatic intermediates compound I and II) so far described for a plant peroxidase and structural alignment suggests that the volume of Ile74 is a factor that influences the solvent accessibility of this important site. A contact between haem C8 vinyl and the sulphur atom of Met37 is observed in the SBP structure. This interaction might affect the stability of the haem group by stabilisation/delocalisation of the porphyrin pi-cation of compound I.

PubMed: 11266599
DOI: 10.1110/ps.37301

Experimental method

X-RAY DIFFRACTION (2.8 Å)