1QGJ

ARABIDOPSIS THALIANA PEROXIDASE N

Summary for 1QGJ

• Entry DOI: 10.2210/pdb1qgj/pdb
• Descriptor: PEROXIDASE N, CALCIUM ION, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total)
• Functional Keywords: peroxidase, oxidoreductase
• Biological source: Arabidopsis thaliana (thale cress)
• Cellular location: Secreted (By similarity): Q39034
• Total number of polymer chains: 2
• Total formula weight: 66012.63

Authors

Mirza, O.,Oestergaard, L.,Welinder, K.G.,Henriksen, A.,Gajhede, M. (deposition date: 1999-04-29, release date: 2000-03-08, Last modification date: 2023-12-27)

Primary citation

Mirza, O.,Henriksen, A.,Ostergaard, L.,Welinder, K.G.,Gajhede, M.
Arabidopsis thaliana peroxidase N: structure of a novel neutral peroxidase.
Acta Crystallogr.,Sect.D, 56:372-375, 2000

PubMed Abstract: The structure of the neutral peroxidase from Arabidopsis thaliana (ATP N) has been determined to a resolution of 1.9 A and a free R value of 20.5%. ATP N has the expected characteristic fold of the class III peroxidases, with a C(alpha) r.m.s.d. of 0.82 A when compared with horseradish peroxidase C (HRP C). HRP C is 54% identical to ATP N in sequence. When the structures of four class III plant peroxidases are superimposed, the regions with structural differences are non-randomly distributed; all are located in one half of the molecule. The architecture of the haem pocket of ATP N is very similar to that of HRP C, in agreement with the low small-molecule substrate specificity of all class III peroxidases. The structure of ATP N suggests that the pH dependence of the substrate turnover will differ from that of HRP C owing to differences in polarity of the residues in the substrate-access channel. Since there are fewer hydrogen bonds to haem C17 propionate O atoms in ATP N than in HRP C, it is suggested that ATP N will lose haem more easily than HRP C. Unlike almost all other class III plant peroxidases, ATP N has a free cysteine residue at a similar position to the suggested secondary substrate-binding site in lignin peroxidase.

PubMed: 10713531
DOI: 10.1107/S0907444999016340

Experimental method

X-RAY DIFFRACTION (1.9 Å)