1ATJ

RECOMBINANT HORSERADISH PEROXIDASE C1A

Summary for 1ATJ

• Entry DOI: 10.2210/pdb1atj/pdb
• Descriptor: PEROXIDASE C1A, CALCIUM ION, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• Functional Keywords: peroxidase, oxidoreductase, glycoprotein
• Biological source: Armoracia rusticana
• Cellular location: Secreted (Probable): P00433
• Total number of polymer chains: 6
• Total formula weight: 206661.62

Authors

Gajhede, M.,Schuller, D.J.,Henriksen, A.,Smith, A.T.,Poulos, T.L. (deposition date: 1997-08-14, release date: 1998-02-04, Last modification date: 2024-10-30)

Primary citation

Gajhede, M.,Schuller, D.J.,Henriksen, A.,Smith, A.T.,Poulos, T.L.
Crystal structure of horseradish peroxidase C at 2.15 A resolution.
Nat.Struct.Biol., 4:1032-1038, 1997

PubMed Abstract: The crystal structure of horseradish peroxidase isozyme C (HRPC) has been solved to 2.15 A resolution. An important feature unique to the class III peroxidases is a long insertion, 34 residues in HRPC, between helices F and G. This region, which defines part of the substrate access channel, is not present in the core conserved fold typical of peroxidases from classes I and II. Comparison of HRPC and peanut peroxidase (PNP), the only other class III (higher plant) peroxidase for which an X-ray structure has been completed, reveals that the structure in this region is highly variable even within class III. For peroxidases of the HRPC type, characterized by a larger FG insertion (seven residues relative to PNP) and a shorter F' helix, we have identified the key residue involved in direct interactions with aromatic donor molecules. HRPC is unique in having a ring of three peripheral Phe residues, 142, 68 and 179. These guard the entrance to the exposed haem edge. We predict that this aromatic region is important for the ability of HRPC to bind aromatic substrates.

PubMed: 9406554
DOI: 10.1038/nsb1297-1032

Experimental method

X-RAY DIFFRACTION (2.15 Å)