Arabidopsis thaliana peroxidase N: structure of a novel neutral peroxidase
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Arabidopsis thaliana peroxidase N : structure of a novel neutral peroxidase. / Mirza, Osman Asghar; Henriksen, A; Ostergaard, L; Welinder, K G; Gajhede, M.
In: Acta Crystallographica. Section D: Biological Crystallography, Vol. 56, No. Pt 3, 03.2000, p. 372-5.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Arabidopsis thaliana peroxidase N
T2 - structure of a novel neutral peroxidase
AU - Mirza, Osman Asghar
AU - Henriksen, A
AU - Ostergaard, L
AU - Welinder, K G
AU - Gajhede, M
PY - 2000/3
Y1 - 2000/3
N2 - 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.
AB - 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.
KW - Amino Acid Sequence
KW - Arabidopsis
KW - Crystallization
KW - Crystallography, X-Ray
KW - Escherichia coli
KW - Models, Molecular
KW - Molecular Sequence Data
KW - Peroxidases
KW - Plant Proteins
KW - Protein Conformation
KW - Recombinant Fusion Proteins
KW - Sequence Alignment
KW - Sequence Homology, Amino Acid
M3 - Journal article
C2 - 10713531
VL - 56
SP - 372
EP - 375
JO - Acta Crystallographica Section D: Structural Biology
JF - Acta Crystallographica Section D: Structural Biology
SN - 2059-7983
IS - Pt 3
ER -
ID: 44864281